2Z22

Crystal structure of phosphate preplasmic binding protein psts from yersinia pestis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.179 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structures of OppA and PstS from Yersinia pestis indicate variability of interactions with transmembrane domains.

Tanabe, M.Mirza, O.Bertrand, T.Atkins, H.S.Titball, R.W.Iwata, S.Brown, K.A.Byrne, B.

(2007) Acta Crystallogr D Biol Crystallogr 63: 1185-1193

  • DOI: https://doi.org/10.1107/S0907444907048299
  • Primary Citation of Related Structures:  
    2Z22, 2Z23

  • PubMed Abstract: 

    Bacterial ATP-binding cassette (ABC) transport systems couple ATP hydrolysis with the uptake and efflux of a wide range of substances across bacterial membranes. These systems are comprised of transmembrane domains, nucleotide binding domains and, in the case of uptake systems, periplasmic binding proteins responsible for binding and presentation of substrate to the transmembrane domains. In pathogenic bacteria, ABC systems are known to play roles in virulence and pathogenicity and the surface localization of some components has made them attractive targets for both vaccine and anti-infective development. Here, the crystallization of five proteins (OppA, PstS, PiuA, YrbD and CysP) from Yersinia pestis, the causative agent of plague, are reported that diffracted to resolution limits ranging from 1.6 to 5 A. The first crystal structures of ABC system components from Y. pestis, OppA and PstS, are also reported here as complexes with their substrates. Comparisons of these two structures with known structures of related proteins suggest that these proteins possess versatility in substrate recognition and variations in protein-protein interactions with their cognate transmembrane domains.


  • Organizational Affiliation

    Membrane Protein Crystallography, Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, England.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Periplasmic phosphate-binding proteinA [auth X],
B [auth A]
321Yersinia pestis CO92Mutation(s): 0 
UniProt
Find proteins for A0A5P8YL10 (Yersinia pestis)
Explore A0A5P8YL10 
Go to UniProtKB:  A0A5P8YL10
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A5P8YL10
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.179 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 68.93α = 90
b = 60.82β = 100.14
c = 78.78γ = 90
Software Package:
Software NamePurpose
CNSrefinement
ADSCdata collection
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-10-30
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.2: 2024-03-13
    Changes: Data collection, Database references, Derived calculations