2GZA

Crystal structure of the VirB11 ATPase from the Brucella Suis type IV secretion system in complex with sulphate

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.238 
  • R-Value Observed: 0.242 

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This is version 1.5 of the entry. See complete history. 


Literature

A Large Domain Swap in the VirB11 ATPase of Brucella suis Leaves the Hexameric Assembly Intact

Hare, S., Bayliss, R., Baron, C., Waksman, G.

(2006) J Mol Biol 360: 56-66

  • DOI: https://doi.org/10.1016/j.jmb.2006.04.060
  • Primary Citation of Related Structures:  
    2GZA

  • PubMed Abstract: 

    VirB11 ATPases are hexameric assemblies that power type IV secretion systems in bacteria. The hexamer of Brucella suis VirB11 (BsB11), like that of the Helicobacter pylori VirB11 (Hp0525), consists of a double ring structure formed by the N-terminal and C-terminal domains of each monomer. However, the monomer differs dramatically from that of Hp0525 by a large domain swap that leaves the hexameric assembly intact but profoundly alters the nucleotide-binding site and the interface between subunits.

    • Organizational Affiliation: 

    School of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Type IV secretion system protein VirB11
A, B, C
361Brucella suis 1330Mutation(s): 0 
Gene Names: VirB11
UniProt
Find proteins for Q8FXK7 (Brucella suis biovar 1 (strain 1330))
Explore Q8FXK7 
Go to UniProtKB:  Q8FXK7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8FXK7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.238 
  • R-Value Observed: 0.242 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 118.211α = 90
b = 125.815β = 90
c = 164.089γ = 90
Software Package:
Software NamePurpose
EPMRphasing
ADSCdata collection
CCP4data scaling
REFMACrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-07-11
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Derived calculations, Source and taxonomy, Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Refinement description
  • Version 1.4: 2018-01-24
    Changes: Structure summary
  • Version 1.5: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description