PDBsum entry 1qun

Go to PDB code: 
protein Protein-protein interface(s) links
Chaperone/structural protein PDB id
Protein chains
(+ 2 more) 200 a.a. *
(+ 2 more) 279 a.a. *
Waters ×64
* Residue conservation analysis
PDB id:
Name: Chaperone/structural protein
Title: X-ray structure of the fimc-fimh chaperone adhesin complex from uropathogenic e.Coli
Structure: Papd-like chaperone fimc. Chain: a, c, e, g, i, k, m, o. Engineered: yes. Mannose-specific adhesin fimh. Chain: b, d, f, h, j, l, n, p. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Biol. unit: Monomer (from PDB file)
2.80Å     R-factor:   0.240     R-free:   0.268
Authors: D.Choudhury,A.Thompson,V.Stojanoff,S.Langerman,J.Pinkner, S.J.Hultgren,S.Knight
Key ref:
D.Choudhury et al. (1999). X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli. Science, 285, 1061-1066. PubMed id: 10446051 DOI: 10.1126/science.285.5430.1061
01-Jul-99     Release date:   31-Aug-99    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P31697  (FIMC_ECOLI) -  Chaperone protein FimC
241 a.a.
200 a.a.*
Protein chains
Pfam   ArchSchema ?
P08191  (FIMH_ECOLI) -  Protein FimH
300 a.a.
279 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     periplasmic space   3 terms 
  Biological process     chaperone-mediated protein folding   4 terms 
  Biochemical function     protein binding involved in protein folding     3 terms  


DOI no: 10.1126/science.285.5430.1061 Science 285:1061-1066 (1999)
PubMed id: 10446051  
X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli.
D.Choudhury, A.Thompson, V.Stojanoff, S.Langermann, J.Pinkner, S.J.Hultgren, S.D.Knight.
Type 1 pili-adhesive fibers expressed in most members of the Enterobacteriaceae family-mediate binding to mannose receptors on host cells through the FimH adhesin. Pilus biogenesis proceeds by way of the chaperone/usher pathway. The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly. The carboxyl-terminal pilin domain of FimH has an immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand complementation mechanism in which the chaperone donates a strand to complete the pilin domain explains the basis for both chaperone function and pilus biogenesis.
  Selected figure(s)  
Figure 1.
Fig. 1. (A) A typical sample of the solvent-flattened experimental electron density map (contoured at 1.0 ) with the refined model superimposed. Arg^8C and Lys^112C anchor the COOH-terminus of FimH (Gln^279H) in the subunit binding cleft of the chaperone through hydrogen bonds to the terminal carboxylate. (B) MOLSCRIPT (24) ribbon diagram of the FimC-FimH complex. FimH is colored yellow, except for the A" (green) and F (orange) strands of the pilin domain. FimC is colored blue, except for the G1 strand, which is cyan. The FimH pilin domain and the NH[2]-terminal domain of FimC form a closed superbarrel with a continuous core made from conserved residues in both proteins. A ball-and-stick representation of the C-HEGA molecule bound to the lectin domain of FimH indicates the position of the carbohydrate-binding site at the tip of the domain.
Figure 4.
Fig. 4. Model of the type 1 pilus. The NH[2]-terminal extension participates in donor strand complementation between subunits as described in the text. Subunits one turn apart in the helix pack against each other through the sides of the pilin barrel. Charged residues located between the hydrophobic side chains in the NH[2]-terminal extension point into the solution on the inside of the hollow pilus rod. (A) The proposed interaction between two consecutive FimA molecules in the type 1 pilus rod. The modeled NH[2]-terminal extension is colored red. (B) View of the pilus from the top. Residue positions that are subject to allelic variation (shown in blue) map to the outer surface of the pilus. (C) Side view of the pilus.
  The above figures are reprinted by permission from the AAAs: Science (1999, 285, 1061-1066) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21344461 C.G.Korea, J.M.Ghigo, and C.Beloin (2011).
The sweet connection: Solving the riddle of multiple sugar-binding fimbrial adhesins in Escherichia coli: Multiple E. coli fimbriae form a versatile arsenal of sugar-binding lectins potentially involved in surface-colonisation and tissue tropism.
  Bioessays, 33, 300-311.  
21091863 C.Giraud, C.S.Bernard, V.Calderon, L.Yang, A.Filloux, S.Molin, G.Fichant, C.Bordi, and Bentzmann (2011).
The PprA-PprB two-component system activates CupE, the first non-archetypal Pseudomonas aeruginosa chaperone-usher pathway system assembling fimbriae.
  Environ Microbiol, 13, 666-683.  
  21472956 C.Grabosch, M.Hartmann, J.Schmidt-Lassen, and T.K.Lindhorst (2011).
Squaric acid monoamide mannosides as ligands for the bacterial lectin FimH: covalent inhibition or not?
  Chembiochem, 12, 1066-1074.  
21637253 G.Phan, H.Remaut, T.Wang, W.J.Allen, K.F.Pirker, A.Lebedev, N.S.Henderson, S.Geibel, E.Volkan, J.Yan, M.B.Kunze, J.S.Pinkner, B.Ford, C.W.Kay, H.Li, S.J.Hultgren, D.G.Thanassi, and G.Waksman (2011).
Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate.
  Nature, 474, 49-53.
PDB codes: 3ohn 3rfz
21404359 K.Vengadesan, and S.V.Narayana (2011).
Structural biology of gram-positive bacterial adhesins.
  Protein Sci, 20, 759-772.  
21299650 N.S.Henderson, T.W.Ng, I.Talukder, and D.G.Thanassi (2011).
Function of the usher N-terminus in catalysing pilus assembly.
  Mol Microbiol, 79, 954-967.  
21088108 S.Felek, J.J.Jeong, L.M.Runco, S.Murray, D.G.Thanassi, and E.S.Krukonis (2011).
Contributions of chaperone/usher systems to cell binding, biofilm formation and Yersinia pestis virulence.
  Microbiology, 157, 805-818.  
20814767 Y.Yang, A.A.Berry, W.C.Lee, J.A.Garnett, J.Marchant, J.A.Levine, P.J.Simpson, S.A.Fogel, K.M.Varney, S.J.Matthews, J.P.Nataro, and K.G.Inman (2011).
Complete (1)H, (13)C and (15)N NMR assignments for donor-strand complemented AafA, the major pilin of aggregative adherence fimbriae (AAF/II) from enteroaggregative E. coli.
  Biomol NMR Assign, 5, 1-5.  
20070257 A.T.Rêgo, V.Chandran, and G.Waksman (2010).
Two-step and one-step secretion mechanisms in Gram-negative bacteria: contrasting the type IV secretion system and the chaperone-usher pathway of pilus biogenesis.
  Biochem J, 425, 475-488.  
20118254 B.Ford, A.T.Rêgo, T.J.Ragan, J.Pinkner, K.Dodson, P.C.Driscoll, S.Hultgren, and G.Waksman (2010).
Structural homology between the C-terminal domain of the PapC usher and its plug.
  J Bacteriol, 192, 1824-1831.
PDB codes: 2kt6 3l48
20478255 I.Le Trong, P.Aprikian, B.A.Kidd, M.Forero-Shelton, V.Tchesnokova, P.Rajagopal, V.Rodriguez, G.Interlandi, R.Klevit, V.Vogel, R.E.Stenkamp, E.V.Sokurenko, and W.E.Thomas (2010).
Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting.
  Cell, 141, 645-655.
PDB code: 3jwn
20378353 K.A.Kline, K.W.Dodson, M.G.Caparon, and S.J.Hultgren (2010).
A tale of two pili: assembly and function of pili in bacteria.
  Trends Microbiol, 18, 224-232.  
20299404 K.Grzymajlo, M.Kuzminska-Bajor, J.Jaworski, P.Dobryszycki, and M.Ugorski (2010).
The high-adhesive properties of the FimH adhesin of Salmonella enterica serovar Enteritidis are determined by a single F118S substitution.
  Microbiology, 156, 1738-1748.  
  20458372 P.Bhomkar, W.Materi, V.Semenchenko, and D.S.Wishart (2010).
Transcriptional response of E. coli upon FimH-mediated fimbrial adhesion.
  Gene Regul Syst Bio, 4, 1.  
20199591 Q.Li, T.W.Ng, K.W.Dodson, S.S.So, K.M.Bayle, J.S.Pinkner, S.Scarlata, S.J.Hultgren, and D.G.Thanassi (2010).
The differential affinity of the usher for chaperone-subunit complexes is required for assembly of complete pili.
  Mol Microbiol, 76, 159-172.  
20067530 S.Shin, and K.S.Kim (2010).
Human brain endothelial ATP synthase beta-subunit is mannose-insensitive binding target of FimH.
  FEMS Microbiol Lett, 303, 156-162.  
20671958 Y.He, Z.Xiang, and H.L.Mobley (2010).
Vaxign: the first web-based vaccine design program for reverse vaccinology and applications for vaccine development.
  J Biomed Biotechnol, 2010, 297505.  
19208633 A.Coddens, M.Diswall, J.Angström, M.E.Breimer, B.Goddeeris, E.Cox, and S.Teneberg (2009).
Recognition of blood group ABH type 1 determinants by the FedF adhesin of F18-fimbriated Escherichia coli.
  J Biol Chem, 284, 9713-9726.  
19629075 B.Ernst, and J.L.Magnani (2009).
From carbohydrate leads to glycomimetic drugs.
  Nat Rev Drug Discov, 8, 661-677.  
  19535913 D.W.Summers, P.M.Douglas, and D.M.Cyr (2009).
Prion propagation by Hsp40 molecular chaperones.
  Prion, 3, 59-64.  
19820722 G.Waksman, and S.J.Hultgren (2009).
Structural biology of the chaperone-usher pathway of pilus biogenesis.
  Nat Rev Microbiol, 7, 765-774.  
19356973 H.Li, and D.G.Thanassi (2009).
Use of a combined cryo-EM and X-ray crystallography approach to reveal molecular details of bacterial pilus assembly by the chaperone/usher pathway.
  Curr Opin Microbiol, 12, 326-332.  
19577575 H.Wang, G.Min, R.Glockshuber, T.T.Sun, and X.P.Kong (2009).
Uropathogenic E. coli adhesin-induced host cell receptor conformational changes: implications in transmembrane signaling transduction.
  J Mol Biol, 392, 352-361.  
19390146 I.Van Molle, K.Moonens, L.Buts, A.Garcia-Pino, S.Panjikar, L.Wyns, H.De Greve, and J.Bouckaert (2009).
The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces.
  Acta Crystallogr D Biol Crystallogr, 65, 411-420.
PDB codes: 3f65 3f6i 3f6l
19903875 J.M.Budzik, C.B.Poor, K.F.Faull, J.P.Whitelegge, C.He, and O.Schneewind (2009).
Intramolecular amide bonds stabilize pili on the surface of bacilli.
  Proc Natl Acad Sci U S A, 106, 19992-19997.
PDB code: 3kpt
19534519 L.H.Liu, H.Dietsch, P.Schurtenberger, and M.Yan (2009).
Photoinitiated coupling of unmodified monosaccharides to iron oxide nanoparticles for sensing proteins and bacteria.
  Bioconjug Chem, 20, 1349-1355.  
19850919 O.S.Mapingire, N.S.Henderson, G.Duret, D.G.Thanassi, and A.H.Delcour (2009).
Modulating effects of the plug, helix, and N- and C-terminal domains on channel properties of the PapC usher.
  J Biol Chem, 284, 36324-36333.  
19734306 S.G.Stahlhut, V.Tchesnokova, C.Struve, S.J.Weissman, S.Chattopadhyay, O.Yakovenko, P.Aprikian, E.V.Sokurenko, and K.A.Krogfelt (2009).
Comparative structure-function analysis of mannose-specific FimH adhesins from Klebsiella pneumoniae and Escherichia coli.
  J Bacteriol, 191, 6592-6601.  
19726681 W.Kress, H.Mutschler, and E.Weber-Ban (2009).
Both ATPase domains of ClpA are critical for processing of stable protein structures.
  J Biol Chem, 284, 31441-31452.  
  19255474 Y.F.Li, S.Poole, F.Rasulova, A.L.McVeigh, S.J.Savarino, and D.Xia (2009).
Crystallization and preliminary X-ray diffraction analyses of several forms of the CfaB major subunit of enterotoxigenic Escherichia coli CFA/I fimbriae.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 242-247.  
19515814 Y.F.Li, S.Poole, K.Nishio, K.Jang, F.Rasulova, A.McVeigh, S.J.Savarino, D.Xia, and E.Bullitt (2009).
Structure of CFA/I fimbriae from enterotoxigenic Escherichia coli.
  Proc Natl Acad Sci U S A, 106, 10793-10798.
PDB codes: 3f83 3f84 3f85
19380723 Y.Huang, B.S.Smith, L.X.Chen, R.H.Baxter, and J.Deisenhofer (2009).
Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC.
  Proc Natl Acad Sci U S A, 106, 7403-7407.
PDB code: 3fip
18446213 A.Wellens, C.Garofalo, H.Nguyen, N.Van Gerven, R.Slättegård, J.P.Hernalsteens, L.Wyns, S.Oscarson, H.De Greve, S.Hultgren, and J.Bouckaert (2008).
Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex.
  PLoS ONE, 3, e2040.
PDB code: 2vco
18400183 C.Puorger, O.Eidam, G.Capitani, D.Erilov, M.G.Grütter, and R.Glockshuber (2008).
Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation.
  Structure, 16, 631-642.
PDB codes: 3bfq 3bfw
18474655 D.A.Rosen, J.S.Pinkner, J.N.Walker, J.S.Elam, J.M.Jones, and S.J.Hultgren (2008).
Molecular variations in Klebsiella pneumoniae and Escherichia coli FimH affect function and pathogenesis in the urinary tract.
  Infect Immun, 76, 3346-3356.  
18803208 D.M.Hatch, A.A.Weiss, R.R.Kale, and S.S.Iyer (2008).
Biotinylated bi- and tetra-antennary glycoconjugates for Escherichia coli detection.
  Chembiochem, 9, 2433-2442.  
18627459 D.Munera, C.Palomino, and L.A.Fernández (2008).
Specific residues in the N-terminal domain of FimH stimulate type 1 fimbriae assembly in Escherichia coli following the initial binding of the adhesin to FimD usher.
  Mol Microbiol, 69, 911-925.  
19000824 D.Verger, R.J.Rose, E.Paci, G.Costakes, T.Daviter, S.Hultgren, H.Remaut, A.E.Ashcroft, S.E.Radford, and G.Waksman (2008).
Structural determinants of polymerization reactivity of the P pilus adaptor subunit PapF.
  Structure, 16, 1724-1731.
PDB code: 2w07
  18854236 E.V.Sokurenko, V.Vogel, and W.E.Thomas (2008).
Catch-bond mechanism of force-enhanced adhesion: counterintuitive, elusive, but ... widespread?
  Cell Host Microbe, 4, 314-323.  
18948113 G.Meng, J.W.St Geme, and G.Waksman (2008).
Repetitive architecture of the Haemophilus influenzae Hia trimeric autotransporter.
  J Mol Biol, 384, 824-836.
PDB codes: 3emf 3emi 3emo
18485872 H.Remaut, C.Tang, N.S.Henderson, J.S.Pinkner, T.Wang, S.J.Hultgren, D.G.Thanassi, G.Waksman, and H.Li (2008).
Fiber formation across the bacterial outer membrane by the chaperone/usher pathway.
  Cell, 133, 640-652.
PDB code: 2vqi
18493664 K.L.Hsu, J.C.Gildersleeve, and L.K.Mahal (2008).
A simple strategy for the creation of a recombinant lectin microarray.
  Mol Biosyst, 4, 654-662.  
18461043 K.T.Forest (2008).
The type II secretion arrowhead: the structure of GspI-GspJ-GspK.
  Nat Struct Mol Biol, 15, 428-430.  
18369105 M.Nishiyama, T.Ishikawa, H.Rechsteiner, and R.Glockshuber (2008).
Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst.
  Science, 320, 376-379.  
18443096 N.Boisen, C.Struve, F.Scheutz, K.A.Krogfelt, and J.P.Nataro (2008).
New adhesin of enteroaggregative Escherichia coli related to the Afa/Dr/AAF family.
  Infect Immun, 76, 3281-3292.  
18292092 O.Yakovenko, S.Sharma, M.Forero, V.Tchesnokova, P.Aprikian, B.Kidd, A.Mach, V.Vogel, E.Sokurenko, and W.E.Thomas (2008).
FimH forms catch bonds that are enhanced by mechanical force due to allosteric regulation.
  J Biol Chem, 283, 11596-11605.  
18668121 R.Fronzes, H.Remaut, and G.Waksman (2008).
Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria.
  EMBO J, 27, 2271-2280.  
18728178 R.J.Rose, D.Verger, T.Daviter, H.Remaut, E.Paci, G.Waksman, A.E.Ashcroft, and S.E.Radford (2008).
Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry.
  Proc Natl Acad Sci U S A, 105, 12873-12878.  
18166195 X.Q.Mu, S.J.Savarino, and E.Bullitt (2008).
The three-dimensional structure of CFA/I adhesion pili: traveler's diarrhea bacteria hang on by a spring.
  J Mol Biol, 376, 614-620.  
17376079 A.V.Zavialov, and S.D.Knight (2007).
A novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1M.
  Mol Microbiol, 64, 153-164.
PDB code: 2os7
17576202 A.Zavialov, G.Zav'yalova, T.Korpela, and V.Zav'yalov (2007).
FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens.
  FEMS Microbiol Rev, 31, 478-514.  
17378923 D.Munera, S.Hultgren, and L.A.Fernández (2007).
Recognition of the N-terminal lectin domain of FimH adhesin by the usher FimD is required for type 1 pilus biogenesis.
  Mol Microbiol, 64, 333-346.  
17511517 D.Verger, E.Bullitt, S.J.Hultgren, and G.Waksman (2007).
Crystal structure of the P pilus rod subunit PapA.
  PLoS Pathog, 3, e73.
PDB codes: 2uy6 2uy7
17359236 G.Bergsten, B.Wullt, M.A.Schembri, I.Leijonhufvud, and C.Svanborg (2007).
Do type 1 fimbriae promote inflammation in the human urinary tract?
  Cell Microbiol, 9, 1766-1781.  
18063798 H.J.Kang, F.Coulibaly, F.Clow, T.Proft, and E.N.Baker (2007).
Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure.
  Science, 318, 1625-1628.
PDB code: 3b2m
17697252 L.M.Nilsson, O.Yakovenko, V.Tchesnokova, W.E.Thomas, M.A.Schembri, V.Vogel, P.Klemm, and E.V.Sokurenko (2007).
The cysteine bond in the Escherichia coli FimH adhesin is critical for adhesion under flow conditions.
  Mol Microbiol, 65, 1158-1169.  
17675342 M.Andersson, B.E.Uhlin, and E.Fällman (2007).
The biomechanical properties of E. coli pili for urinary tract attachment reflect the host environment.
  Biophys J, 93, 3008-3014.  
18059531 M.Zhao, X.Jia, C.Wang, Q.Li, K.Zhou, L.Wang, H.Liu, and S.Peng (2007).
PAK: an essential motif for forming beta-turn structures and exhibiting the thrombolytic effect of P6A and its analogs.
  Biochem Cell Biol, 85, 730-740.  
17222190 N.A.Khan, Y.Kim, S.Shin, and K.S.Kim (2007).
FimH-mediated Escherichia coli K1 invasion of human brain microvascular endothelial cells.
  Cell Microbiol, 9, 169-178.  
18041905 P.Klemm, V.Hancock, M.Kvist, and M.A.Schembri (2007).
Candidate targets for new antivirulence drugs: selected cases of bacterial adhesion and biofilm formation.
  Future Microbiol, 2, 643-653.  
17022032 R.J.Pieters (2007).
Intervention with bacterial adhesion by multivalent carbohydrates.
  Med Res Rev, 27, 796-816.  
18063717 S.P.Nuccio, and A.J.Bäumler (2007).
Evolution of the chaperone/usher assembly pathway: fimbrial classification goes Greek.
  Microbiol Mol Biol Rev, 71, 551-575.  
17293418 S.Ruer, S.Stender, A.Filloux, and Bentzmann (2007).
Assembly of fimbrial structures in Pseudomonas aeruginosa: functionality and specificity of chaperone-usher machineries.
  J Bacteriol, 189, 3547-3555.  
17302815 S.T.Poole, A.L.McVeigh, R.P.Anantha, L.H.Lee, Y.M.Akay, E.A.Pontzer, D.A.Scott, E.Bullitt, and S.J.Savarino (2007).
Donor strand complementation governs intersubunit interaction of fimbriae of the alternate chaperone pathway.
  Mol Microbiol, 63, 1372-1384.  
17551629 V.Aberg, and F.Almqvist (2007).
Pilicides-small molecules targeting bacterial virulence.
  Org Biomol Chem, 5, 1827-1834.  
17496084 Y.M.Lee, K.W.Dodson, and S.J.Hultgren (2007).
Adaptor function of PapF depends on donor strand exchange in P-pilus biogenesis of Escherichia coli.
  J Bacteriol, 189, 5276-5283.  
16982834 D.A.Chalton, J.A.Musson, H.Flick-Smith, N.Walker, A.McGregor, H.K.Lamb, E.D.Williamson, J.Miller, J.H.Robinson, and J.H.Lakey (2006).
Immunogenicity of a Yersinia pestis vaccine antigen monomerized by circular permutation.
  Infect Immun, 74, 6624-6631.  
17082819 D.Verger, E.Miller, H.Remaut, G.Waksman, and S.Hultgren (2006).
Molecular mechanism of P pilus termination in uropathogenic Escherichia coli.
  EMBO Rep, 7, 1228-1232.
PDB code: 2j2z
16785325 G.Min, H.Wang, T.T.Sun, and X.P.Kong (2006).
Structural basis for tetraspanin functions as revealed by the cryo-EM structure of uroplakin complexes at 6-A resolution.
  J Cell Biol, 173, 975-983.  
16828554 H.Remaut, and G.Waksman (2006).
Protein-protein interaction through beta-strand addition.
  Trends Biochem Sci, 31, 436-444.  
16793551 H.Remaut, R.J.Rose, T.J.Hannan, S.J.Hultgren, S.E.Radford, A.E.Ashcroft, and G.Waksman (2006).
Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism.
  Mol Cell, 22, 831-842.
PDB codes: 2cny 2cnz 2co1 2co2 2co3 2co4 2co6 2co7
17098869 J.S.Pinkner, H.Remaut, F.Buelens, E.Miller, V.Aberg, N.Pemberton, M.Hedenström, A.Larsson, P.Seed, G.Waksman, S.J.Hultgren, and F.Almqvist (2006).
Rationally designed small compounds inhibit pilus biogenesis in uropathogenic bacteria.
  Proc Natl Acad Sci U S A, 103, 17897-17902.
PDB code: 2j7l
17661687 K.J.Wright, and S.J.Hultgren (2006).
Sticky fibers and uropathogenesis: bacterial adhesins in the urinary tract.
  Future Microbiol, 1, 75-87.  
16235261 K.S.Rotondi, and L.M.Gierasch (2006).
Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins.
  Biopolymers, 84, 13-22.  
  17142917 M.De Kerpel, I.Van Molle, L.Brys, L.Wyns, H.De Greve, and J.Bouckaert (2006).
N-terminal truncation enables crystallization of the receptor-binding domain of the FedF bacterial adhesin.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1278-1282.  
17047869 M.Dubber, O.Sperling, and T.K.Lindhorst (2006).
Oligomannoside mimetics by glycosylation of 'octopus glycosides' and their investigation as inhibitors of type 1 fimbriae-mediated adhesion of Escherichia coli.
  Org Biomol Chem, 4, 3901-3912.  
16933977 M.Forero, O.Yakovenko, E.V.Sokurenko, W.E.Thomas, and V.Vogel (2006).
Uncoiling mechanics of Escherichia coli type I fimbriae are optimized for catch bonds.
  PLoS Biol, 4, e298.  
16767077 M.Vetsch, D.Erilov, N.Molière, M.Nishiyama, O.Ignatov, and R.Glockshuber (2006).
Mechanism of fibre assembly through the chaperone-usher pathway.
  EMBO Rep, 7, 734-738.  
17047870 O.Sperling, A.Fuchs, and T.K.Lindhorst (2006).
Evaluation of the carbohydrate recognition domain of the bacterial adhesin FimH: Design, synthesis and binding properties of mannoside ligands.
  Org Biomol Chem, 4, 3913-3922.  
16421447 R.Jedrzejczak, Z.Dauter, M.Dauter, R.Piatek, B.Zalewska, M.Mróz, K.Bury, B.Nowicki, and J.Kur (2006).
Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails.
  Acta Crystallogr D Biol Crystallogr, 62, 157-164.
PDB code: 2axw
16573686 S.S.So, and D.G.Thanassi (2006).
Analysis of the requirements for pilus biogenesis at the outer membrane usher and the function of the usher C-terminus.
  Mol Microbiol, 60, 364-375.  
17073155 V.A.Beskhlebnaya, E.V.Trinchina, P.Aprikyan, V.Chesnokova, and E.V.Sokurenko (2006).
Molecular genetic analysis of Escherichia coli type I adhesins.
  Bull Exp Biol Med, 141, 339-342.  
16272438 W.Thomas, M.Forero, O.Yakovenko, L.Nilsson, P.Vicini, E.Sokurenko, and V.Vogel (2006).
Catch-bond model derived from allostery explains force-activated bacterial adhesion.
  Biophys J, 90, 753-764.  
16782819 X.Q.Mu, and E.Bullitt (2006).
Structure and assembly of P-pili: a protruding hinge region used for assembly of a bacterial adhesion filament.
  Proc Natl Acad Sci U S A, 103, 9861-9866.  
15834497 B.S.Kim, W.Y.Yang, J.H.Ryu, Y.S.Yoo, and M.Lee (2005).
Carbohydrate-coated nanocapsules from amphiphilic rod-coil molecule: binding to bacterial type 1 pili.
  Chem Commun (Camb), (), 2035-2037.  
15592451 E.Fällman, S.Schedin, J.Jass, B.E.Uhlin, and O.Axner (2005).
The unfolding of the P pili quaternary structure by stretching is reversible, not plastic.
  EMBO Rep, 6, 52-56.  
  16511060 I.Van Molle, L.Buts, F.Coppens, L.Qiang, L.Wyns, R.Loris, J.Bouckaert, and H.De Greve (2005).
Crystallization of the FaeE chaperone of Escherichia coli F4 fimbriae.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 427-431.  
15659162 J.Bouckaert, J.Berglund, M.Schembri, E.De Genst, L.Cools, M.Wuhrer, C.S.Hung, J.Pinkner, R.Slättegård, A.Zavialov, D.Choudhury, S.Langermann, S.J.Hultgren, L.Wyns, P.Klemm, S.Oscarson, S.D.Knight, and H.De Greve (2005).
Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin.
  Mol Microbiol, 55, 441-455.
PDB codes: 1tr7 1uwf
15569242 J.M.Bower, D.S.Eto, and M.A.Mulvey (2005).
Covert operations of uropathogenic Escherichia coli within the urinary tract.
  Traffic, 6, 18-31.  
16040975 M.A.Schembri, J.Blom, K.A.Krogfelt, and P.Klemm (2005).
Capsule and fimbria interaction in Klebsiella pneumoniae.
  Infect Immun, 73, 4626-4633.  
16294247 M.Hedenström, H.Emtenäs, N.Pemberton, V.Aberg, S.J.Hultgren, J.S.Pinkner, V.Tegman, F.Almqvist, I.Sethson, and J.Kihlberg (2005).
NMR studies of interactions between periplasmic chaperones from uropathogenic E. coli and pilicides that interfere with chaperone function and pilus assembly.
  Org Biomol Chem, 3, 4193-4200.  
15968039 M.Kostakioti, C.L.Newman, D.G.Thanassi, and C.Stathopoulos (2005).
Mechanisms of protein export across the bacterial outer membrane.
  J Bacteriol, 187, 4306-4314.  
15920478 M.Nishiyama, R.Horst, O.Eidam, T.Herrmann, O.Ignatov, M.Vetsch, P.Bettendorff, I.Jelesarov, M.G.Grütter, K.Wüthrich, R.Glockshuber, and G.Capitani (2005).
Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD.
  EMBO J, 24, 2075-2086.
PDB codes: 1zdv 1zdx 1ze3
16183020 M.Pellecchia (2005).
Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions.
  Chem Biol, 12, 961-971.  
15618148 R.Piatek, B.Zalewska, O.Kolaj, M.Ferens, B.Nowicki, and J.Kur (2005).
Molecular aspects of biogenesis of Escherichia coli Dr Fimbriae: characterization of DraB-DraE complexes.
  Infect Immun, 73, 135-145.  
16240004 V.Aberg, M.Hedenström, J.S.Pinkner, S.J.Hultgren, and F.Almqvist (2005).
C-Terminal properties are important for ring-fused 2-pyridones that interfere with the chaperone function in uropathogenic E. coli.
  Org Biomol Chem, 3, 3886-3892.  
14760735 F.Rosenau, J.Tommassen, and K.E.Jaeger (2004).
Lipase-specific foldases.
  Chembiochem, 5, 152-161.  
15093830 H.Remaut, and G.Waksman (2004).
Structural biology of bacterial pathogenesis.
  Curr Opin Struct Biol, 14, 161-170.  
15583129 J.G.Bann, J.S.Pinkner, C.Frieden, and S.J.Hultgren (2004).
Catalysis of protein folding by chaperones in pathogenic bacteria.
  Proc Natl Acad Sci U S A, 101, 17389-17393.  
15327779 K.L.Anderson, J.Billington, D.Pettigrew, E.Cota, P.Simpson, P.Roversi, H.A.Chen, P.Urvil, L.du Merle, P.N.Barlow, M.E.Medof, R.A.Smith, B.Nowicki, C.Le Bouguénec, S.M.Lea, and S.Matthews (2004).
An atomic resolution model for assembly, architecture, and function of the Dr adhesins.
  Mol Cell, 15, 647-657.
PDB code: 1rxl
15455180 M.R.Wehner, S.R.Koch, L.Kindinger, N.Nelson, and M.M.Cowan (2004).
Asparaginase inhibition of adhesion of type 1-fimbriated and P-fimbriated Escherichia coli to epithelial cell receptors.
  Appl Microbiol Biotechnol, 66, 71-73.  
15372038 M.Vetsch, C.Puorger, T.Spirig, U.Grauschopf, E.U.Weber-Ban, and R.Glockshuber (2004).
Pilus chaperones represent a new type of protein-folding catalyst.
  Nature, 431, 329-333.  
15375127 P.Khandelwal, D.Choudhury, A.Birah, M.K.Reddy, G.P.Gupta, and N.Banerjee (2004).
Insecticidal pilin subunit from the insect pathogen Xenorhabdus nematophila.
  J Bacteriol, 186, 6465-6476.  
15292133 T.W.Ng, L.Akman, M.Osisami, and D.G.Thanassi (2004).
The usher N terminus is the initial targeting site for chaperone-subunit complexes and participates in subsequent pilus biogenesis events.
  J Bacteriol, 186, 5321-5331.  
15205435 Y.M.Lee, P.A.DiGiuseppe, T.J.Silhavy, and S.J.Hultgren (2004).
P pilus assembly motif necessary for activation of the CpxRA pathway by PapE in Escherichia coli.
  J Bacteriol, 186, 4326-4337.  
12654838 A.Smeds, M.Pertovaara, T.Timonen, T.Pohjanvirta, S.Pelkonen, and A.Palva (2003).
Mapping the binding domain of the F18 fimbrial adhesin.
  Infect Immun, 71, 2163-2172.  
12787500 A.V.Zavialov, J.Berglund, A.F.Pudney, L.J.Fooks, T.M.Ibrahim, S.MacIntyre, and S.D.Knight (2003).
Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation.
  Cell, 113, 587-596.
PDB codes: 1p5u 1p5v
12554953 A.Zavialov, J.Berglund, and S.D.Knight (2003).
Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the F1 antigen Caf1M-Caf1 chaperone-subunit pre-assembly complex from Yersinia pestis.
  Acta Crystallogr D Biol Crystallogr, 59, 359-362.  
12949111 E.Veiga, Lorenzo, and L.A.Fernández (2003).
Autotransporters as scaffolds for novel bacterial adhesins: surface properties of Escherichia coli cells displaying Jun/Fos dimerization domains.
  J Bacteriol, 185, 5585-5590.  
12761149 F.Hommais, S.Gouriou, C.Amorin, H.Bui, M.C.Rahimy, B.Picard, and E.Denamur (2003).
The FimH A27V mutation is pathoadaptive for urovirulence in Escherichia coli B2 phylogenetic group isolates.
  Infect Immun, 71, 3619-3622.  
14567919 K.Ponnuraj, M.G.Bowden, S.Davis, S.Gurusiddappa, D.Moore, D.Choe, Y.Xu, M.Hook, and S.V.Narayana (2003).
A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen.
  Cell, 115, 217-228.
PDB codes: 1r17 1r19
12864853 L.Buts, J.Bouckaert, E.De Genst, R.Loris, S.Oscarson, M.Lahmann, J.Messens, E.Brosens, L.Wyns, and H.De Greve (2003).
The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine.
  Mol Microbiol, 49, 705-715.
PDB codes: 1o9v 1o9w 1o9z
12777763 L.Buts, R.Loris, E.De Genst, S.Oscarson, M.Lahmann, J.Messens, E.Brosens, L.Wyns, H.De Greve, and J.Bouckaert (2003).
Solving the phase problem for carbohydrate-binding proteins using selenium derivatives of their ligands: a case study involving the bacterial F17-G adhesin.
  Acta Crystallogr D Biol Crystallogr, 59, 1012-1015.  
12700251 M.M.Barnhart, F.G.Sauer, J.S.Pinkner, and S.J.Hultgren (2003).
Chaperone-subunit-usher interactions required for donor strand exchange during bacterial pilus assembly.
  J Bacteriol, 185, 2723-2730.  
12787495 S.Behrens (2003).
Periplasmic chaperones--preservers of subunit folding energy for organelle assembly.
  Cell, 113, 556-557.  
12648942 S.J.Weissman, S.L.Moseley, D.E.Dykhuizen, and E.V.Sokurenko (2003).
Enterobacterial adhesins and the case for studying SNPs in bacteria.
  Trends Microbiol, 11, 115-117.  
12180918 A.V.Zavialov, J.Kersley, T.Korpela, V.P.Zav'yalov, S.MacIntyre, and S.D.Knight (2002).
Donor strand complementation mechanism in the biogenesis of non-pilus systems.
  Mol Microbiol, 45, 983-995.  
12485987 C.C.Deivanayagam, E.R.Wann, W.Chen, M.Carson, K.R.Rajashankar, M.Höök, and S.V.Narayana (2002).
A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A.
  EMBO J, 21, 6660-6672.
PDB code: 1n67
12270835 C.H.Jones, P.Dexter, A.K.Evans, C.Liu, S.J.Hultgren, and D.E.Hruby (2002).
Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin.
  J Bacteriol, 184, 5762-5771.  
12010488 C.S.Hung, J.Bouckaert, D.Hung, J.Pinkner, C.Widberg, A.DeFusco, C.G.Auguste, R.Strouse, S.Langermann, G.Waksman, and S.J.Hultgren (2002).
Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection.
  Mol Microbiol, 44, 903-915.
PDB codes: 1kiu 1klf
12399496 D.G.Thanassi, C.Stathopoulos, K.Dodson, D.Geiger, and S.J.Hultgren (2002).
Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis.
  J Bacteriol, 184, 6260-6269.  
12437927 F.G.Sauer, J.S.Pinkner, G.Waksman, and S.J.Hultgren (2002).
Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation.
  Cell, 111, 543-551.
PDB codes: 1n0l 1n12
11792867 J.G.Bann, J.Pinkner, S.J.Hultgren, and C.Frieden (2002).
Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD.
  Proc Natl Acad Sci U S A, 99, 709-714.  
12107137 K.Kjaergaard, H.Hasman, M.A.Schembri, and P.Klemm (2002).
Antigen 43-mediated autotransporter display, a versatile bacterial cell surface presentation system.
  J Bacteriol, 184, 4197-4204.  
12037304 S.D.Knight, D.Choudhury, S.Hultgren, J.Pinkner, V.Stojanoff, and A.Thompson (2002).
Structure of the S pilus periplasmic chaperone SfaE at 2.2 A resolution.
  Acta Crystallogr D Biol Crystallogr, 58, 1016-1022.
PDB code: 1l4i
12110187 W.E.Thomas, E.Trintchina, M.Forero, V.Vogel, and E.V.Sokurenko (2002).
Bacterial adhesion to target cells enhanced by shear force.
  Cell, 109, 913-923.  
12169612 X.Q.Mu, E.H.Egelman, and E.Bullitt (2002).
Structure and function of Hib pili from Haemophilus influenzae type b.
  J Bacteriol, 184, 4868-4874.  
11948880 A.Svensson, A.Larsson, H.Emtenäs, M.Hedenström, T.Fex, S.J.Hultgren, J.S.Pinkner, F.Almqvist, and J.Kihlberg (2001).
Design and evaluation of pilicides: potential novel antibacterial agents directed against uropathogenic Escherichia coli.
  Chembiochem, 2, 915-918.  
11282637 A.V.Zavialov, N.V.Batchikova, T.Korpela, L.E.Petrovskaya, V.G.Korobko, J.Kersley, S.MacIntyre, and V.P.Zav'yalov (2001).
Secretion of recombinant proteins via the chaperone/usher pathway in Escherichia coli.
  Appl Environ Microbiol, 67, 1805-1814.  
11598031 B.K.Choi, and D.M.Schifferli (2001).
Characterization of FasG segments required for 987P fimbria-mediated binding to piglet glycoprotein receptors.
  Infect Immun, 69, 6625-6632.  
11461995 C.Cobbold, M.Windsor, and T.Wileman (2001).
A virally encoded chaperone specialized for folding of the major capsid protein of African swine fever virus.
  J Virol, 75, 7221-7229.  
11285215 D.L.Hung, T.L.Raivio, C.H.Jones, T.J.Silhavy, and S.J.Hultgren (2001).
Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili.
  EMBO J, 20, 1508-1518.  
11532135 E.V.Sokurenko, M.A.Schembri, E.Trintchina, K.Kjaergaard, D.L.Hasty, and P.Klemm (2001).
Valency conversion in the type 1 fimbrial adhesin of Escherichia coli.
  Mol Microbiol, 41, 675-686.  
11171011 J.D.Schilling, M.A.Mulvey, and S.J.Hultgren (2001).
Structure and function of Escherichia coli type 1 pili: new insight into the pathogenesis of urinary tract infections.
  J Infect Dis, 183, S36-S40.  
11133944 J.Tanskanen, S.Saarela, S.Tankka, N.Kalkkinen, M.Rhen, T.K.Korhonen, and B.Westerlund-Wikström (2001).
The gaf fimbrial gene cluster of Escherichia coli expresses a full-size and a truncated soluble adhesin protein.
  J Bacteriol, 183, 512-519.  
11440716 K.W.Dodson, J.S.Pinkner, T.Rose, G.Magnusson, S.J.Hultgren, and G.Waksman (2001).
Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor.
  Cell, 105, 733-743.
PDB codes: 1j8r 1j8s
11580845 M.A.Schembri, G.Christiansen, and P.Klemm (2001).
FimH-mediated autoaggregation of Escherichia coli.
  Mol Microbiol, 41, 1419-1430.  
11171009 M.A.Schembri, K.Kjaergaard, E.V.Sokurenko, and P.Klemm (2001).
Molecular characterization of the Escherichia coli FimH adhesin.
  J Infect Dis, 183, S28-S31.  
11406584 M.A.Schembri, and P.Klemm (2001).
Coordinate gene regulation by fimbriae-induced signal transduction.
  EMBO J, 20, 3074-3081.  
11179294 M.A.Schembri, and P.Klemm (2001).
Biofilm formation in a hydrodynamic environment by novel fimh variants and ramifications for virulence.
  Infect Immun, 69, 1322-1328.  
  11454740 M.A.Sung, K.Fleming, H.A.Chen, and S.Matthews (2001).
The solution structure of PapGII from uropathogenic Escherichia coli and its recognition of glycolipid receptors.
  EMBO Rep, 2, 621-627.  
11274473 P.M.Harrison, H.S.Chan, S.B.Prusiner, and F.E.Cohen (2001).
Conformational propagation with prion-like characteristics in a simple model of protein folding.
  Protein Sci, 10, 819-835.  
11395476 S.L.Harris, P.A.Spears, E.A.Havell, T.S.Hamrick, J.R.Horton, and P.E.Orndorff (2001).
Characterization of Escherichia coli type 1 pilus mutants with altered binding specificities.
  J Bacteriol, 183, 4099-4102.  
10873830 D.G.Thanassi, and S.J.Hultgren (2000).
Multiple pathways allow protein secretion across the bacterial outer membrane.
  Curr Opin Cell Biol, 12, 420-430.  
10908657 E.T.Saulino, E.Bullitt, and S.J.Hultgren (2000).
Snapshots of usher-mediated protein secretion and ordered pilus assembly.
  Proc Natl Acad Sci U S A, 97, 9240-9245.  
11042452 F.G.Sauer, M.Barnhart, D.Choudhury, S.D.Knight, G.Waksman, and S.J.Hultgren (2000).
Chaperone-assisted pilus assembly and bacterial attachment.
  Curr Opin Struct Biol, 10, 548-556.  
10736261 F.G.Sauer, S.D.Knight, G.J.Waksman and, and S.J.Hultgren (2000).
PapD-like chaperones and pilus biogenesis.
  Semin Cell Dev Biol, 11, 27-34.  
10760135 G.P.Krasan, F.G.Sauer, D.Cutter, M.M.Farley, J.R.Gilsdorf, S.J.Hultgren, and J.W.St Geme (2000).
Evidence for donor strand complementation in the biogenesis of Haemophilus influenzae haemagglutinating pili.
  Mol Microbiol, 35, 1335-1347.  
  10933504 I.Callebaut, D.Gilgès, I.Vigon, and J.P.Mornon (2000).
HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold.
  Protein Sci, 9, 1382-1390.  
  11206055 J.F.Kreisberg, S.D.Betts, and J.King (2000).
Beta-helix core packing within the triple-stranded oligomerization domain of the P22 tailspike.
  Protein Sci, 9, 2338-2343.  
10856226 J.J.Martinez, M.A.Mulvey, J.D.Schilling, J.S.Pinkner, and S.J.Hultgren (2000).
Type 1 pilus-mediated bacterial invasion of bladder epithelial cells.
  EMBO J, 19, 2803-2812.  
10922042 M.A.Mulvey, J.D.Schilling, J.J.Martinez, and S.J.Hultgren (2000).
Bad bugs and beleaguered bladders: interplay between uropathogenic Escherichia coli and innate host defenses.
  Proc Natl Acad Sci U S A, 97, 8829-8835.  
10768955 M.A.Schembri, E.V.Sokurenko, and P.Klemm (2000).
Functional flexibility of the FimH adhesin: insights from a random mutant library.
  Infect Immun, 68, 2638-2646.  
10913698 M.A.Schembri, H.Hasman, and P.Klemm (2000).
Expression and purification of the mannose recognition domain of the FimH adhesin.
  FEMS Microbiol Lett, 188, 147-151.  
10859353 M.M.Barnhart, J.S.Pinkner, G.E.Soto, F.G.Sauer, S.Langermann, G.Waksman, C.Frieden, and S.J.Hultgren (2000).
PapD-like chaperones provide the missing information for folding of pilin proteins.
  Proc Natl Acad Sci U S A, 97, 7709-7714.  
10655518 R.A.Edwards, D.M.Schifferli, and S.R.Maloy (2000).
A role for Salmonella fimbriae in intraperitoneal infections.
  Proc Natl Acad Sci U S A, 97, 1258-1262.  
10884397 S.Normark (2000).
Anfinsen comes out of the cage during assembly of the bacterial pilus.
  Proc Natl Acad Sci U S A, 97, 7670-7672.  
10869080 T.S.Hamrick, S.L.Harris, P.A.Spears, E.A.Havell, J.R.Horton, P.W.Russell, and P.E.Orndorff (2000).
Genetic characterization of Escherichia coli type 1 pilus adhesin mutants and identification of a novel binding phenotype.
  J Bacteriol, 182, 4012-4021.  
10995223 U.Hermanns, P.Sebbel, V.Eggli, and R.Glockshuber (2000).
Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli.
  Biochemistry, 39, 11564-11570.  
10736262 U.Shinde, and M.Inouye (2000).
Intramolecular chaperones: polypeptide extensions that modulate protein folding.
  Semin Cell Dev Biol, 11, 35-44.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.