2X49

Crystal structure of the C-terminal domain of InvA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.225 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.193 

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This is version 1.1 of the entry. See complete history


Literature

Crystal Structure of the C-Terminal Domain of the Salmonella Type III Secretion System Export Apparatus Protein Inva.

Worrall, L.J.Vuckovic, M.Strynadka, N.C.J.

(2010) Protein Sci 19: 1091

  • DOI: https://doi.org/10.1002/pro.382
  • Primary Citation of Related Structures:  
    2X49, 2X4A

  • PubMed Abstract: 

    InvA is a prominent inner-membrane component of the Salmonella type III secretion system (T3SS) apparatus, which is responsible for regulating virulence protein export in pathogenic bacteria. InvA is made up of an N-terminal integral membrane domain and a C-terminal cytoplasmic domain that is proposed to form part of a docking platform for the soluble export apparatus proteins notably the T3SS ATPase InvC. Here, we report the novel crystal structure of the C-terminal domain of Salmonella InvA which shows a compact structure composed of four subdomains. The overall structure is unique although the first and second subdomains exhibit structural similarity to the peripheral stalk of the A/V-type ATPase and a ring building motif found in other T3SS proteins respectively.


  • Organizational Affiliation

    Centre for Blood Research, Department of Biochemistry and Molecular Biology, University of British Columbia, Life Sciences Centre, British Columbia, Canada V6T 1Z3.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
INVASION PROTEIN INVA333Salmonella enterica subsp. enterica serovar Typhimurium str. LT2Mutation(s): 0 
UniProt
Find proteins for P0A1I3 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
Explore P0A1I3 
Go to UniProtKB:  P0A1I3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A1I3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.225 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.193 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 44.991α = 90
b = 57.413β = 90
c = 113.87γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
autoSHARPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-03-31
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance