1D2O

CRYSTAL STRUCTURE OF A SINGLE B REPEAT UNIT (B1) OF COLLAGEN BINDING SURFACE PROTEIN (CNA) OF STAPHYLOCOCCUS AUREUS.

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.212 
  • R-Value Observed: 0.212 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Novel fold and assembly of the repetitive B region of the Staphylococcus aureus collagen-binding surface protein.

Deivanayagam, C.C., Rich, R.L., Carson, M., Owens, R.T., Danthuluri, S., Bice, T., Hook, M., Narayana, S.V.

(2000) Structure 8: 67-78

  • DOI: https://doi.org/10.1016/s0969-2126(00)00081-2
  • Primary Citation of Related Structures:  
    1D2O, 1D2P

  • PubMed Abstract: 

    [corrected] The Staphylococcus aureus collagen-binding protein Cna mediates bacterial adherence to collagen. The primary sequence of Cna has a non-repetitive collagen-binding A region, followed by the repetitive B region. The B region has one to four 23 kDa repeat units (B(1)-B(4)), depending on the strain of origin. The affinity of the A region for collagen is independent of the B region. However, the B repeat units have been suggested to serve as a 'stalk' that projects the A region from the bacterial surface and thus facilitate bacterial adherence to collagen. To understand the biological role of these B-region repeats we determined their three-dimensional structure.

    • Organizational Affiliation: 

    Center for Macromolecular Crystallography, School of Optometry, University of Alabama at Birmingham, Birmingham, AL 35294-0005, USA.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
COLLAGEN ADHESIN
A, B
187Staphylococcus aureusMutation(s): 0 
UniProt
Find proteins for Q53654 (Staphylococcus aureus)
Explore Q53654 
Go to UniProtKB:  Q53654
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ53654
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.212 
  • R-Value Observed: 0.212 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 96.907α = 90
b = 101.538β = 90
c = 121γ = 90
Software Package:
Software NamePurpose
CNSrefinement
PHASESphasing
XTALVIEWrefinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-09-27
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-07-24
    Changes: Data collection, Refinement description
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references