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PDBsum entry 1omp

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Periplasmic binding protein PDB id
1omp

 

 

 

 

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Contents
Protein chain
370 a.a. *
Waters ×73
* Residue conservation analysis
PDB id:
1omp
Name: Periplasmic binding protein
Title: Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin-binding protein involved in active transport and chemotaxis
Structure: D-maltodextrin binding protein. Chain: a. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562.
Resolution:
1.80Å     R-factor:   0.210    
Authors: A.J.Sharff,F.A.Quiocho
Key ref:
A.J.Sharff et al. (1992). Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry, 31, 10657-10663. PubMed id: 1420181 DOI: 10.1021/bi00159a003
Date:
14-Sep-92     Release date:   31-Jan-94    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0AEX9  (MALE_ECOLI) -  Maltose/maltodextrin-binding periplasmic protein from Escherichia coli (strain K12)
Seq:
Struc:
396 a.a.
370 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1021/bi00159a003 Biochemistry 31:10657-10663 (1992)
PubMed id: 1420181  
 
 
Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis.
A.J.Sharff, L.E.Rodseth, J.C.Spurlino, F.A.Quiocho.
 
  ABSTRACT  
 
The periplasmic maltodextrin binding protein of Escherichia coli serves as an initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. The three-dimensional structure of the binding protein complexed with maltose has been previously reported [Spurlino, J. C., Lu, G.-Y., & Quiocho, F. A. (1991) J. Biol. Chem. 266, 5202-5219]. Here we report the structure of the unliganded form of the binding protein refined to 1.8-A resolution. This structure, combined with that for the liganded form, provides the first crystallographic evidence that a major ligand-induced conformational change occurs in a periplasmic binding protein. The unliganded structure shows a rigid-body "hinge-bending" between the two globular domains by approximately 35 degrees, relative to the maltose-bound structure, opening the sugar binding site groove located between the two domains. In addition, there is an 8 degrees twist of one domain relative to the other domain. The conformational changes observed between this structure and the maltose-bound structure are consistent with current models of maltose/maltodextrin transport and maltose chemotaxis and solidify a mechanism for receptor differentiation between the ligand-free and ligand-bound forms in signal transduction.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21194366 B.C.Chu, and H.J.Vogel (2011).
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PDB code: 3pgf
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18851580 A.Paciaroni, A.Orecchini, E.Cornicchi, M.Marconi, C.Petrillo, M.Haertlein, M.Moulin, H.Schober, M.Tarek, and F.Sacchetti (2008).
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Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR.
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Crystal structure of a catalytic intermediate of the maltose transporter.
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Structural basis for cyclodextrin recognition by Thermoactinomyces vulgaris cyclo/maltodextrin-binding protein.
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Binding of the viral immunogenic octapeptide VSV8 to native glucose-regulated protein Grp94 (gp96) and its inhibition by the physiological ligands ATP and Ca2+.
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A salt-bridge motif involved in ligand binding and large-scale domain motions of the maltose-binding protein.
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Large-scale prediction of protein geometry and stability changes for arbitrary single point mutations.
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15308642 A.Schiefner, G.Holtmann, K.Diederichs, W.Welte, and E.Bremer (2004).
Structural basis for the binding of compatible solutes by ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus.
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PDB codes: 1sw1 1sw2 1sw4 1sw5
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Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport.
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Identification of common structural features of binding sites in galactose-specific proteins.
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FhuD1, a ferric hydroxamate-binding lipoprotein in Staphylococcus aureus: a case of gene duplication and lateral transfer.
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Crystal structures of fusion proteins with large-affinity tags.
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PDB codes: 1n4a 1n4d
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Super-channel in bacteria: function and structure of a macromolecule import system mediated by a pit-dependent ABC transporter.
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Super-channel in bacteria: function and structure of the macromolecule import system mediated by a pit-dependent ABC transporter.
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Substrate binding stabilizes S-adenosylhomocysteine hydrolase in a closed conformation.
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Biochemistry, physiology and pathophysiology of the extracellular calcium-sensing receptor.
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Acarbose, a pseudooligosaccharide, is transported but not metabolized by the maltose-maltodextrin system of Escherichia coli.
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Structural principles governing domain motions in proteins.
  Proteins, 36, 425-435.  
  10452613 S.Sheshadri, G.M.Lingaraju, and R.Varadarajan (1999).
Denaturant mediated unfolding of both native and molten globule states of maltose binding protein are accompanied by large deltaCp's.
  Protein Sci, 8, 1689-1695.  
9927672 Y.Zhang, P.J.Gardina, A.S.Kuebler, H.S.Kang, J.A.Christopher, and M.D.Manson (1999).
Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism.
  Proc Natl Acad Sci U S A, 96, 939-944.  
  10072081 B.Sandak, R.Nussinov, and H.J.Wolfson (1998).
A method for biomolecular structural recognition and docking allowing conformational flexibility.
  J Comput Biol, 5, 631-654.  
9651355 D.G.Vassylyev, H.Tomitori, K.Kashiwagi, K.Morikawa, and K.Igarashi (1998).
Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificity.
  J Biol Chem, 273, 17604-17609.
PDB code: 1a99
9761835 D.G.Vassylyev, T.Kashiwagi, H.Tomitori, K.Kashiwagi, K.Igarashi, and K.Morikawa (1998).
Crystallization and preliminary X-ray analysis of the periplasmic receptor (PotF) of the putrescine transport system in Escherichia coli.
  Acta Crystallogr D Biol Crystallogr, 54, 132-134.  
9862806 D.M.Lawson, C.E.Williams, L.A.Mitchenall, and R.N.Pau (1998).
Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA.
  Structure, 6, 1529-1539.
PDB code: 1atg
9535871 J.M.Betton, N.Sassoon, M.Hofnung, and M.Laurent (1998).
Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli.
  J Biol Chem, 273, 8897-8902.  
  9573146 M.Pajatsch, M.Gerhart, R.Peist, R.Horlacher, W.Boos, and A.Böck (1998).
The periplasmic cyclodextrin binding protein CymE from Klebsiella oxytoca and its role in maltodextrin and cyclodextrin transport.
  J Bacteriol, 180, 2630-2635.  
9687374 M.S.Jurica, and B.L.Stoddard (1998).
Mind your B's and R's: bacterial chemotaxis, signal transduction and protein recognition.
  Structure, 6, 809-813.  
9843405 N.Campobasso, C.A.Costello, C.Kinsland, T.P.Begley, and S.E.Ealick (1998).
Crystal structure of thiaminase-I from Bacillus thiaminolyticus at 2.0 A resolution.
  Biochemistry, 37, 15981-15989.
PDB codes: 2thi 3thi 4thi
  9792100 S.Raffy, N.Sassoon, M.Hofnung, and J.M.Betton (1998).
Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein.
  Protein Sci, 7, 2136-2142.  
  9529892 W.Boos, and H.Shuman (1998).
Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation.
  Microbiol Mol Biol Rev, 62, 204-229.  
9013553 B.X.Yan, and Y.Q.Sun (1997).
Glycine residues provide flexibility for enzyme active sites.
  J Biol Chem, 272, 3190-3194.  
9125524 C.Ganesh, A.N.Shah, C.P.Swaminathan, A.Surolia, and R.Varadarajan (1997).
Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein.
  Biochemistry, 36, 5020-5028.  
9201949 D.Chamberlain, B.P.O'Hara, S.A.Wilson, L.H.Pearl, and S.J.Perkins (1997).
Oligomerization of the amide sensor protein AmiC by x-ray and neutron scattering and molecular modeling.
  Biochemistry, 36, 8020-8029.  
9309217 F.A.Quiocho, J.C.Spurlino, and L.E.Rodseth (1997).
Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor.
  Structure, 5, 997.
PDB codes: 1anf 3mbp 4mbp
9037707 F.A.Saul, B.Vulliez-le Normand, F.Lema, and G.A.Bentley (1997).
Crystal structure of a recombinant form of the maltodextrin-binding protein carrying an inserted sequence of a B-cell epitope from the preS2 region of hepatitis B virus.
  Proteins, 27, 1-8.
PDB code: 1iud
9095676 G.E.Arnold, and R.L.Ornstein (1997).
Protein hinge bending as seen in molecular dynamics simulations of native and M61 mutant T4 lysozymes.
  Biopolymers, 41, 533-544.  
9188448 G.Richarme, and T.D.Caldas (1997).
Chaperone properties of the bacterial periplasmic substrate-binding proteins.
  J Biol Chem, 272, 15607-15612.  
9211908 J.A.Hall, K.Gehring, and H.Nikaido (1997).
Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein.
  J Biol Chem, 272, 17605-17609.  
9211909 J.A.Hall, T.E.Thorgeirsson, J.Liu, Y.K.Shin, and H.Nikaido (1997).
Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling.
  J Biol Chem, 272, 17610-17614.  
9442881 J.J.Falke, R.B.Bass, S.L.Butler, S.A.Chervitz, and M.A.Danielson (1997).
The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes.
  Annu Rev Cell Dev Biol, 13, 457-512.  
9359111 J.M.Betton, J.P.Jacob, M.Hofnung, and J.K.Broome-Smith (1997).
Creating a bifunctional protein by insertion of beta-lactamase into the maltodextrin-binding protein.
  Nat Biotechnol, 15, 1276-1279.  
9113995 J.S.Marvin, E.E.Corcoran, N.A.Hattangadi, J.V.Zhang, S.A.Gere, and H.W.Hellinga (1997).
The rational design of allosteric interactions in a monomeric protein and its applications to the construction of biosensors.
  Proc Natl Acad Sci U S A, 94, 4366-4371.  
9345630 J.Trewhella (1997).
Insights into biomolecular function from small-angle scattering.
  Curr Opin Struct Biol, 7, 702-708.  
9245406 S.H.Sleigh, J.R.Tame, E.J.Dodson, and A.J.Wilkinson (1997).
Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine.
  Biochemistry, 36, 9747-9758.
PDB codes: 1rkm 2rkm
  9070445 S.Szmelcman, N.Sassoon, and M.Hofnung (1997).
Residues in the alpha helix 7 of the bacterial maltose binding protein which are important in interactions with the Mal FGK2 complex.
  Protein Sci, 6, 628-636.  
9370432 T.B.Woolf (1997).
Molecular dynamics of individual alpha-helices of bacteriorhodopsin in dimyristol phosphatidylocholine. I. Structure and dynamics.
  Biophys J, 73, 2376-2392.  
  9111326 T.E.Blank, M.P.Woods, C.M.Lebo, P.Xin, and J.E.Hopper (1997).
Novel Gal3 proteins showing altered Gal80p binding cause constitutive transcription of Gal4p-activated genes in Saccharomyces cerevisiae.
  Mol Cell Biol, 17, 2566-2575.  
  9007986 V.Novokhatny, and K.Ingham (1997).
Thermodynamics of maltose binding protein unfolding.
  Protein Sci, 6, 141-146.  
8702898 A.Wolf, K.C.Lee, J.F.Kirsch, and G.F.Ames (1996).
Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity.
  J Biol Chem, 271, 21243-21250.  
8861200 F.A.Quiocho, and P.S.Ledvina (1996).
Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes.
  Mol Microbiol, 20, 17-25.  
8662800 G.F.Ames, C.E.Liu, A.K.Joshi, and K.Nikaido (1996).
Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases.
  J Biol Chem, 271, 14264-14270.  
8727319 G.V.Louie, P.D.Brownlie, R.Lambert, J.B.Cooper, T.L.Blundell, S.P.Wood, V.N.Malashkevich, A.Hädener, M.J.Warren, and P.M.Shoolingin-Jordan (1996).
The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-A resolution.
  Proteins, 25, 48-78.  
8800468 M.A.Danielson, and J.J.Falke (1996).
Use of 19F NMR to probe protein structure and conformational changes.
  Annu Rev Biophys Biomol Struct, 25, 163-195.  
  8897598 S.Sugiyama, Y.Matsuo, K.Maenaka, D.G.Vassylyev, M.Matsushima, K.Kashiwagi, K.Igarashi, and K.Morikawa (1996).
The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding.
  Protein Sci, 5, 1984-1990.
PDB code: 1pot
8663400 Y.Zhang, D.E.Mannering, A.L.Davidson, N.Yao, and M.D.Manson (1996).
Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis.
  J Biol Chem, 271, 17881-17889.  
8749361 A.M.Stock, and S.L.Mowbray (1995).
Bacterial chemotaxis: a field in motion.
  Curr Opin Struct Biol, 5, 744-751.  
7608172 A.Wolf, E.W.Shaw, B.H.Oh, H.De Bondt, A.K.Joshi, and G.F.Ames (1995).
Structure/function analysis of the periplasmic histidine-binding protein. Mutations decreasing ligand binding alter the properties of the conformational change and of the closed form.
  J Biol Chem, 270, 16097-16106.  
7893717 C.L.Careaga, J.Sutherland, J.Sabeti, and J.J.Falke (1995).
Large amplitude twisting motions of an interdomain hinge: a disulfide trapping study of the galactose-glucose binding protein.
  Biochemistry, 34, 3048-3055.  
8747465 J.R.Tame, E.J.Dodson, G.Murshudov, C.F.Higgins, and A.J.Wilkinson (1995).
The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands.
  Structure, 3, 1395-1406.
PDB codes: 1olc 2olb
7553867 M.A.Schumacher, K.Y.Choi, F.Lu, H.Zalkin, and R.G.Brennan (1995).
Mechanism of corepressor-mediated specific DNA binding by the purine repressor.
  Cell, 83, 147-155.
PDB code: 1dbq
7784427 M.D.Paulsen, and R.L.Ornstein (1995).
Dramatic differences in the motions of the mouth of open and closed cytochrome P450BM-3 by molecular dynamics simulations.
  Proteins, 21, 237-243.  
  8528088 S.Trakhanov, and F.A.Quiocho (1995).
Influence of divalent cations in protein crystallization.
  Protein Sci, 4, 1914-1919.  
  7795522 W.R.Cannon, J.M.Briggs, J.Shen, J.A.McCammon, and F.A.Quiocho (1995).
Conservative and nonconservative mutations in proteins: anomalous mutations in a transport receptor analyzed by free energy and quantum chemical calculations.
  Protein Sci, 4, 387-393.  
  8062817 A.Vrielink, W.Rüger, H.P.Driessen, and P.S.Freemont (1994).
Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose.
  EMBO J, 13, 3413-3422.
PDB codes: 1bgt 1bgu 2bgt 2bgu
7813489 B.Schwermann, K.Pfau, B.Liliensiek, M.Schleyer, T.Fischer, and E.P.Bakker (1994).
Purification, properties and structural aspects of a thermoacidophilic alpha-amylase from Alicyclobacillus acidocaldarius atcc 27009. Insight into acidostability of proteins.
  Eur J Biochem, 226, 981-991.  
7529124 J.Jäger, S.J.Smerdon, J.Wang, D.C.Boisvert, and T.A.Steitz (1994).
Comparison of three different crystal forms shows HIV-1 reverse transcriptase displays an internal swivel motion.
  Structure, 2, 869-876.  
  8157012 K.M.Covitz, C.H.Panagiotidis, L.I.Hor, M.Reyes, N.A.Treptow, and H.A.Shuman (1994).
Mutations that alter the transmembrane signalling pathway in an ATP binding cassette (ABC) transporter.
  EMBO J, 13, 1752-1759.  
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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