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PDBsum entry 1kap
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Zinc metalloprotease PDB id
1kap

 

 

 

 

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Contents
Protein chain
470 a.a. *
Ligands
GLY-SER-ASN-SER
Metals
_CA ×8
_ZN
Waters ×292
* Residue conservation analysis
PDB id:
1kap
Name: Zinc metalloprotease
Title: Three-dimensional structure of the alkaline protease of pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif
Structure: Alkaline protease. Chain: p. Synonym: p. Aeruginosa alkaline protease. Tetrapeptide (gly ser asn ser). Chain: i
Source: Pseudomonas aeruginosa. Organism_taxid: 208964. Strain: pao1. Strain: pao1
Resolution:
1.64Å     R-factor:   0.176    
Authors: U.Baumann,S.Wu,K.M.Flaherty,D.B.Mckay
Key ref: U.Baumann et al. (1993). Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. Embo J, 12, 3357-3364. PubMed id: 8253063
Date:
08-Jun-95     Release date:   15-Oct-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q03023  (APRA_PSEAE) -  Serralysin from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Seq:
Struc: 		479 a.a.
470 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.24.40  - serralysin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage of bonds with hydrophobic residues in P1'.
      Cofactor: Zn(2+)

 

 
Embo J 12:3357-3364 (1993)
PubMed id: 8253063  
 
 
Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif.
U.Baumann, S.Wu, K.M.Flaherty, D.B.McKay.
 
  ABSTRACT  
 
The three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa, a zinc metalloprotease, has been solved to a resolution of 1.64 A by multiple isomorphous replacement and non-crystallographic symmetry averaging between different crystal forms. The molecule is elongated with overall dimensions of 90 x 35 x 25 A; it has two distinct structural domains. The N-terminal domain is the proteolytic domain; it has an overall tertiary fold and active site zinc ligation similar to that of astacin, a metalloprotease isolated from a European freshwater crayfish. The C-terminal domain consists of a 21-strand beta sandwich. Within this domain is a novel 'parallel beta roll' structure in which successive beta strands are wound in a right-handed spiral, and in which Ca2+ ions are bound within the turns between strands by a repeated GGXGXD sequence motif, a motif that is found in a diverse group of proteins secreted by Gram-negative bacteria.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21482800 C.P.Garnham, R.L.Campbell, and P.L.Davies (2011).
Anchored clathrate waters bind antifreeze proteins to ice.
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PDB code: 3p4g
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20823309 A.Vo, N.Nguyen, and H.Huang (2010).
Solenoid and non-solenoid protein recognition using stationary wavelet packet transform.
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20530907 C.Yang, F.Wang, J.Hao, K.Zhang, N.Yuan, and M.Sun (2010).
Identification of a proteolytic bacterium, HW08, and characterization of its extracellular cold-active alkaline metalloprotease Ps5.
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Protein tandem repeats - the more perfect, the less structured.
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Mutations affecting the extreme C terminus of Escherichia coli haemolysin A reduce haemolytic activity by altering the folding of the toxin.
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19015266 A.Chenal, J.I.Guijarro, B.Raynal, M.Delepierre, and D.Ladant (2009).
RTX Calcium Binding Motifs Are Intrinsically Disordered in the Absence of Calcium: IMPLICATION FOR PROTEIN SECRETION.
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19558324 A.E.Oberholzer, M.Bumann, T.Hege, S.Russo, and U.Baumann (2009).
Metzincin's canonical methionine is responsible for the structural integrity of the zinc-binding site.
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PDB codes: 3hb2 3hbu 3hbv 3hda
19255155 A.Tang, M.E.Marquart, J.D.Fratkin, C.C.McCormick, A.R.Caballero, H.P.Gatlin, and R.J.O'Callaghan (2009).
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Catalytic domain architecture of metzincin metalloproteases.
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18987131 K.Kuwahara, C.Angkawidjaja, H.Matsumura, Y.Koga, K.Takano, and S.Kanaya (2008).
Importance of the Ca2+-binding sites in the N-catalytic domain of a family I.3 lipase for activity and stability.
  Protein Eng Des Sel, 21, 737-744.
PDB codes: 2zj6 2zj7
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18378637 L.Li, J.L.Rock, and D.R.Nelson (2008).
Identification and characterization of a repeat-in-toxin gene cluster in Vibrio anguillarum.
  Infect Immun, 76, 2620-2632.  
19019219 L.P.Tripathi, and R.Sowdhamini (2008).
Genome-wide survey of prokaryotic serine proteases: analysis of distribution and domain architectures of five serine protease families in prokaryotes.
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18713318 M.Ramjeet, A.D.Cox, M.A.Hancock, M.Mourez, J.Labrie, M.Gottschalk, and M.Jacques (2008).
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  Mol Microbiol, 70, 221-235.  
17908326 A.J.Scotter, M.Guo, M.M.Tomczak, M.E.Daley, R.L.Campbell, R.J.Oko, D.A.Bateman, A.Chakrabartty, B.D.Sykes, and P.L.Davies (2007).
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PDB codes: 2z8r 2z8s
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MARTX, multifunctional autoprocessing repeats-in-toxin toxins.
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PDB codes: 2qua 2qub
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Cold-active enzymes studied by comparative molecular dynamics simulation.
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NMR structure of the R-module: a parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase.
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PDB code: 2agm
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Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN.
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Membrane insertion of Escherichia coli alpha-hemolysin is independent from membrane lysis.
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Pore-forming and enzymatic activities of Bordetella pertussis adenylate cyclase toxin synergize in promoting lysis of monocytes.
  Infect Immun, 74, 2207-2214.  
16913841 N.R.Matheson, J.Potempa, and J.Travis (2006).
Interaction of a novel form of Pseudomonas aeruginosa alkaline protease (aeruginolysin) with interleukin-6 and interleukin-8.
  Biol Chem, 387, 911-915.  
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Purification and characterization of a hemolysin-like protein, Sll1951, a nontoxic member of the RTX protein family from the Cyanobacterium Synechocystis sp. strain PCC 6803.
  J Bacteriol, 188, 3535-3542.  
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Mutations in HlyD, part of the type 1 translocator for hemolysin secretion, affect the folding of the secreted toxin.
  J Bacteriol, 187, 7471-7480.  
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CHDL: a cadherin-like domain in Proteobacteria and Cyanobacteria.
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16221305 P.Walasek, and J.F.Honek (2005).
Nonnatural amino acid incorporation into the methionine 214 position of the metzincin Pseudomonas aeruginosa alkaline protease.
  BMC Biochem, 6, 21.  
15143215 A.V.Kajava, U.Baxa, R.B.Wickner, and A.C.Steven (2004).
A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure.
  Proc Natl Acad Sci U S A, 101, 7885-7890.  
14765110 H.Nummelin, M.C.Merckel, J.C.Leo, H.Lankinen, M.Skurnik, and A.Goldman (2004).
The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll.
  EMBO J, 23, 701-711.
PDB code: 1p9h
15385451 M.Kostakioti, and C.Stathopoulos (2004).
Functional analysis of the Tsh autotransporter from an avian pathogenic Escherichia coli strain.
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Purification and cloning of an endogenous protein inhibitor of carp nephrosin, an astacin metalloproteinase.
  J Biol Chem, 279, 11146-11155.  
12582172 A.L.Cortajarena, F.M.Goni, and H.Ostolaza (2003).
A receptor-binding region in Escherichia coli alpha-haemolysin.
  J Biol Chem, 278, 19159-19163.  
12694917 D.J.Rigden, M.J.Jedrzejas, and M.Y.Galperin (2003).
An extracellular calcium-binding domain in bacteria with a distant relationship to EF-hands.
  FEMS Microbiol Lett, 221, 103-110.  
12577270 N.Aghajari, F.Van Petegem, V.Villeret, J.P.Chessa, C.Gerday, R.Haser, and J.Van Beeumen (2003).
Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases.
  Proteins, 50, 636-647.
PDB codes: 1g9k 1h71
12707273 R.E.Feltzer, J.O.Trent, and R.D.Gray (2003).
Alkaline proteinase inhibitor of Pseudomonas aeruginosa: a mutational and molecular dynamics study of the role of N-terminal residues in the inhibition of Pseudomonas alkaline proteinase.
  J Biol Chem, 278, 25952-25957.  
12890017 S.M.Hinsa, M.Espinosa-Urgel, J.L.Ramos, and G.A.O'Toole (2003).
Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein.
  Mol Microbiol, 49, 905-918.  
12837794 S.Ravaud, P.Gouet, R.Haser, and N.Aghajari (2003).
Probing the role of divalent metal ions in a bacterial psychrophilic metalloprotease: binding studies of an enzyme in the crystalline state by x-ray crystallography.
  J Bacteriol, 185, 4195-4203.
PDB codes: 1o0q 1o0t 1om6 1om7 1om8 1omj
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His-859 is an essential residue for the activity and pH dependence of Escherichia coli RTX toxin alpha-hemolysin.
  J Biol Chem, 277, 23223-23229.  
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Caulobacter crescentus synthesizes an S-layer-editing metalloprotease possessing a domain sharing sequence similarity with its paracrystalline S-layer protein.
  J Bacteriol, 184, 2709-2718.  
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The N terminus of the HasA protein and the SecB chaperone cooperate in the efficient targeting and secretion of HasA via the ATP-binding cassette transporter.
  J Biol Chem, 277, 6726-6732.  
16233181 H.J.Kwon, M.Haruki, M.Morikawa, K.Omori, and S.Kanaya (2002).
Role of repetitive nine-residue sequence motifs in secretion, enzymatic activity, and protein conformation of a family I.3 lipase.
  J Biosci Bioeng, 93, 157-164.  
11827810 J.Michiels, C.Xi, J.Verhaert, and J.Vanderleyden (2002).
The functions of Ca(2+) in bacteria: a role for EF-hand proteins?
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Disease-causing mutations in cartilage oligomeric matrix protein cause an unstructured Ca2+ binding domain.
  J Biol Chem, 277, 10581-10589.  
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Membrane interaction of Escherichia coli hemolysin: flotation and insertion-dependent labeling by phospholipid vesicles.
  J Bacteriol, 183, 5364-5370.  
11168421 C.Schindel, A.Zitzer, B.Schulte, A.Gerhards, P.Stanley, C.Hughes, V.Koronakis, S.Bhakdi, and M.Palmer (2001).
Interaction of Escherichia coli hemolysin with biological membranes. A study using cysteine scanning mutagenesis.
  Eur J Biochem, 268, 800-808.  
11316870 J.D.Cronk, J.A.Endrizzi, M.R.Cronk, J.W.O'neill, and K.Y.Zhang (2001).
Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.
  Protein Sci, 10, 911-922.
PDB codes: 1i6o 1i6p
11721016 M.J.Kuiper, P.L.Davies, and V.K.Walker (2001).
A theoretical model of a plant antifreeze protein from Lolium perenne.
  Biophys J, 81, 3560-3565.
PDB code: 1i3b
11118599 M.V.Ramstadab, S.Markussen, T.E.Ellingsen, G.Skjåk-Braek, and D.W.Levine (2001).
Influence of environmental conditions on the activity of the recombinant mannuronan C-5-epimerase AlgE2.
  Enzyme Microb Technol, 28, 57-69.  
11223512 T.Hori, T.Kumasaka, M.Yamamoto, N.Nonaka, N.Tanaka, Y.Hashimoto, U.Ueki, and K.Takio (2001).
Structure of a new 'aspzincin' metalloendopeptidase from Grifola frondosa: implications for the catalytic mechanism and substrate specificity based on several different crystal forms.
  Acta Crystallogr D Biol Crystallogr, 57, 361-368.
PDB codes: 1g12 1ge5 1ge6 1ge7
11050437 B.Kobe, and A.V.Kajava (2000).
When protein folding is simplified to protein coiling: the continuum of solenoid protein structures.
  Trends Biochem Sci, 25, 509-515.  
10737931 B.Schuler, F.Fürst, F.Osterroth, S.Steinbacher, R.Huber, and R.Seckler (2000).
Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein.
  Proteins, 39, 89.
PDB codes: 1qq1 1qrb 1qrc
10671437 E.Hoiczyk, and A.Hansel (2000).
Cyanobacterial cell walls: news from an unusual prokaryotic envelope.
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11243259 H.K.Høidal, B.I.Glaerum Svanem, M.Gimmestad, and S.Valla (2000).
Mannuronan C-5 epimerases and cellular differentiation of Azotobacter vinelandii.
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Do parallel beta-helix proteins have a unique fourier transform infrared spectrum?
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10975518 T.A.Springer, H.Jing, and J.Takagi (2000).
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Secretion of the Caulobacter crescentus S-layer protein: further localization of the C-terminal secretion signal and its use for secretion of recombinant proteins.
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Insertion of Escherichia coli alpha-haemolysin in lipid bilayers as a non-transmembrane integral protein: prediction and experiment.
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The A modules of the Azotobacter vinelandii mannuronan-C-5-epimerase AlgE1 are sufficient for both epimerization and binding of Ca2+.
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Identification of a member of the serralysin family isolated from a psychrotrophic bacterium, Pseudomonas fluorescens 114.
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Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing.
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10581355 J.Young, and I.B.Holland (1999).
ABC transporters: bacterial exporters-revisited five years on.
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10361285 K.E.Walker, S.Moghaddame-Jafari, C.V.Lockatell, D.Johnson, and R.Belas (1999).
ZapA, the IgA-degrading metalloprotease of Proteus mirabilis, is a virulence factor expressed specifically in swarmer cells.
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10215870 N.Izadi-Pruneyre, N.Wolff, V.Redeker, C.Wandersman, M.Delepierre, and A.Lecroisey (1999).
NMR studies of the C-terminal secretion signal of the haem-binding protein, HasA.
  Eur J Biochem, 261, 562-568.  
  10225859 S.J.Lee, M.C.Gray, L.Guo, P.Sebo, and E.L.Hewlett (1999).
Epitope mapping of monoclonal antibodies against Bordetella pertussis adenylate cyclase toxin.
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Reversible denaturation, self-aggregation, and membrane activity of Escherichia coli alpha-hemolysin, a protein stable in 6 M urea.
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Characterization of Rhizobium leguminosarum exopolysaccharide glycanases that are secreted via a type I exporter and have a novel heptapeptide repeat motif.
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The active site structure of tetanus neurotoxin resolved by multiple scattering analysis in X-Ray absorption spectroscopy.
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Analysis of zinc binding sites in protein crystal structures.
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Distinct mechanisms for K+ efflux, intoxication, and hemolysis by Bordetella pertussis AC toxin.
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The S-layer protein from Campylobacter rectus: sequence determination and function of the recombinant protein.
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Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa.
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Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function.
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9187652 A.S.Robinson, and J.King (1997).
Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein.
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9241431 C.Chothia, T.Hubbard, S.Brenner, H.Barns, and A.Murzin (1997).
Protein folds in the all-beta and all-alpha classes.
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  9009299 C.Kooi, R.S.Hodges, and P.A.Sokol (1997).
Identification of neutralizing epitopes on Pseudomonas aeruginosa elastase and effects of cross-reactions on other thermolysin-like proteases.
  Infect Immun, 65, 472-477.  
  9385650 V.Villeret, J.P.Chessa, C.Gerday, and J.Van Beeumen (1997).
Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile Pseudomonas aeruginosa.
  Protein Sci, 6, 2462-2464.  
9201942 W.Hu, G.Van Driessche, B.Devreese, C.F.Goodhew, D.F.McGinnity, N.Saunders, V.Fulop, G.W.Pettigrew, and J.J.Van Beeumen (1997).
Structural characterization of Paracoccus denitrificans cytochrome c peroxidase and assignment of the low and high potential heme sites.
  Biochemistry, 36, 7958-7966.  
9125517 W.L.Mock, and J.Yao (1997).
Kinetic characterization of the serralysins: a divergent catalytic mechanism pertaining to astacin-type metalloproteases.
  Biochemistry, 36, 4949-4958.  
8814237 A.M.Moura-da-Silva, G.D.Laing, M.J.Paine, J.M.Dennison, V.Politi, J.M.Crampton, and R.D.Theakston (1996).
Processing of pro-tumor necrosis factor-alpha by venom metalloproteinases: a hypothesis explaining local tissue damage following snake bite.
  Eur J Immunol, 26, 2000-2005.  
8692845 B.Brahamsha (1996).
An abundant cell-surface polypeptide is required for swimming by the nonflagellated marine cyanobacterium Synechococcus.
  Proc Natl Acad Sci U S A, 93, 6504-6509.  
8946845 B.Kobe (1996).
Leucines on a roll.
  Nat Struct Biol, 3, 977-980.  
8756323 F.Grams, V.Dive, A.Yiotakis, I.Yiallouros, S.Vassiliou, R.Zwilling, W.Bode, and W.Stöcker (1996).
Structure of astacin with a transition-state analogue inhibitor.
  Nat Struct Biol, 3, 671-675.
PDB codes: 1qji 1qjj
8900122 N.Kita, C.M.Boyd, M.R.Garrett, F.Jurnak, and N.T.Keen (1996).
Differential effect of site-directed mutations in pelC on pectate lyase activity, plant tissue maceration, and elicitor activity.
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8654408 S.Morante, L.Furenlid, G.Schiavo, F.Tonello, R.Zwilling, and C.Montecucco (1996).
X-ray absorption spectroscopy study of zinc coordination in tetanus neurotoxin, astacin, alkaline protease and thermolysin.
  Eur J Biochem, 235, 606-612.  
8855221 S.Steinbacher, U.Baxa, S.Miller, A.Weintraub, R.Seckler, and R.Huber (1996).
Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.
  Proc Natl Acad Sci U S A, 93, 10584-10588.
PDB codes: 1tyu 1tyv 1tyw 1tyx
8740360 V.Dhanaraj, Q.Z.Ye, L.L.Johnson, D.J.Hupe, D.F.Ortwine, J.B.Dunbar, J.R.Rubin, A.Pavlovsky, C.Humblet, and T.L.Blundell (1996).
X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily.
  Structure, 4, 375-386.  
8710874 Z.Y.Zhu, and S.Karlin (1996).
Clusters of charged residues in protein three-dimensional structures.
  Proc Natl Acad Sci U S A, 93, 8350-8355.  
7583641 B.Kobe, and J.Deisenhofer (1995).
Proteins with leucine-rich repeats.
  Curr Opin Struct Biol, 5, 409-416.  
8771234 C.Montecucco, and G.Schiavo (1995).
Structure and function of tetanus and botulinum neurotoxins.
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8561847 D.Soler, T.Nomizu, W.E.Brown, Y.Shibata, and D.S.Auld (1995).
Matrilysin: expression, purification, and characterization.
  J Protein Chem, 14, 511-520.  
9156583 G.Menestrina, M.Dalla Serra, C.Pederzolli, M.Bregante, and F.Gambale (1995).
Bacterial hemolysins and leukotoxins affect target cells by forming large exogenous pores into their plasma membrane: Escherichia coli hemolysin A as a case example.
  Biosci Rep, 15, 543-551.  
  7883008 H.Ostolaza, A.Soloaga, and F.M.Goñi (1995).
The binding of divalent cations to Escherichia coli alpha-haemolysin.
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7581298 O.Rossetto, F.Deloye, B.Poulain, R.Pellizzari, G.Schiavo, and C.Montecucco (1995).
The metallo-proteinase activity of tetanus and botulism neurotoxins.
  J Physiol Paris, 89, 43-50.  
7583673 P.T.Lansbury, P.R.Costa, J.M.Griffiths, E.J.Simon, M.Auger, K.J.Halverson, D.A.Kocisko, Z.S.Hendsch, T.T.Ashburn, and R.G.Spencer (1995).
Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide.
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8575448 R.Gilmour, S.Prazeres, D.F.McGinnity, C.F.Goodhew, J.J.Moura, I.Moura, and G.W.Pettigrew (1995).
The affinity and specificity of Ca(2+)-binding sites of cytochrome-c peroxidase from Paracoccus denitrificans.
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7588817 S.Harada, T.Kinoshita, N.Kasai, S.Tsunasawa, and F.Sakiyama (1995).
Complete amino acid sequence of a zinc metalloendoprotease from Streptomyces caespitosus.
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7552726 T.E.Benson, D.J.Filman, C.T.Walsh, and J.M.Hogle (1995).
An enzyme-substrate complex involved in bacterial cell wall biosynthesis.
  Nat Struct Biol, 2, 644-653.
PDB code: 1mbr
7592850 T.Rose, P.Sebo, J.Bellalou, and D.Ladant (1995).
Interaction of calcium with Bordetella pertussis adenylate cyclase toxin. Characterization of multiple calcium-binding sites and calcium-induced conformational changes.
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8539248 V.Sieber, F.Jurnak, and G.R.Moe (1995).
Circular dichroism of the parallel beta helical proteins pectate lyase C and E.
  Proteins, 23, 32-37.  
  7663339 W.Stöcker, F.Grams, U.Baumann, P.Reinemer, F.X.Gomis-Rüth, D.B.McKay, and W.Bode (1995).
The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases.
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7583637 W.Stöcker, and W.Bode (1995).
Structural features of a superfamily of zinc-endopeptidases: the metzincins.
  Curr Opin Struct Biol, 5, 383-390.  
7817399 B.Kobe, and J.Deisenhofer (1994).
The leucine-rich repeat: a versatile binding motif.
  Trends Biochem Sci, 19, 415-421.  
  7516312 C.Kooi, A.Cox, P.Darling, and P.A.Sokol (1994).
Neutralizing monoclonal antibodies to an extracellular Pseudomonas cepacia protease.
  Infect Immun, 62, 2811-2817.  
7712282 F.Jurnak, M.D.Yoder, R.Pickersgill, and J.Jenkins (1994).
Parallel beta-domains: a new fold in protein structures.
  Curr Opin Struct Biol, 4, 802-806.  
7984032 G.Menestrina, G.Schiavo, and C.Montecucco (1994).
Molecular mechanisms of action of bacterial protein toxins.
  Mol Aspects Med, 15, 79.  
  8188585 H.Ertesvåg, B.Doseth, B.Larsen, G.Skjåk-Braek, and S.Valla (1994).
Cloning and expression of an Azotobacter vinelandii mannuronan C-5-epimerase gene.
  J Bacteriol, 176, 2846-2853.  
7922035 J.Janin (1994).
Proteins with a ring.
  Structure, 2, 571-573.  
7851740 S.K.Kochi, G.Schiavo, M.Mock, and C.Montecucco (1994).
Zinc content of the Bacillus anthracis lethal factor.
  FEMS Microbiol Lett, 124, 343-348.  
  8137810 W.Bode, P.Reinemer, R.Huber, T.Kleine, S.Schnierer, and H.Tschesche (1994).
The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.
  EMBO J, 13, 1263-1269.
PDB code: 1jap
  7960097 Y.Duan, E.Fisher, D.Malamud, E.Golub, and D.R.Demuth (1994).
Calcium-binding properties of SSP-5, the Streptococcus gordonii M5 receptor for salivary agglutinin.
  Infect Immun, 62, 5220-5226.  
8081735 C.Chothia, and A.G.Murzin (1993).
New folds for all-beta proteins.
  Structure, 1, 217-222.  
8081738 M.D.Yoder, S.E.Lietzke, and F.Jurnak (1993).
Unusual structural features in the parallel beta-helix in pectate lyases.
  Structure, 1, 241-251.
PDB code: 1pcl
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 code is shown on the right.

 

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