3GZ1

Crystal structure of IpgC in complex with the chaperone binding region of IpaB

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.201 

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


Literature

IpaB-IpgC interaction defines binding motif for type III secretion translocator

Lunelli, M., Lokareddy, R.K., Zychlinsky, A., Kolbe, M.

(2009) Proc Natl Acad Sci U S A 106: 9661-9666

  • DOI: https://doi.org/10.1073/pnas.0812900106
  • Primary Citation of Related Structures:  
    3GYZ, 3GZ1

  • PubMed Abstract: 

    The delivery of virulence factors into host cells through type III secretion systems is essential for enterobacterial pathogenesis. Molecular chaperones bind specifically to virulence factors in the bacterial cytosol before secretion. Invasion plasmid gene C (IpgC) is a chaperone that binds 2 essential virulence factors of Shigella: invasion plasmid antigens (Ipa) B and C. Here, we report the crystal structure of IpgC alone and in complex with the chaperone binding domain (CBD) of IpaB. The chaperone captures the CBD in an extended conformation that is stabilized by conserved residues lining the cleft. Analysis of the cocrystal structure reveals a sequence motif that is functional in the IpaB translocator class from different bacteria as determined by isothermal titration calorimetry. Our results show how translocators are chaperoned and may allow the design of inhibitors of enterobacterial diseases.

    • Organizational Affiliation: 

    Department of Cellular Microbiology, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chaperone protein ipgC
A, B
151Shigella flexneriMutation(s): 1 
Gene Names: ipgC
UniProt
Find proteins for P0A2U4 (Shigella flexneri)
Explore P0A2U4 
Go to UniProtKB:  P0A2U4
Entity Groups  
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UniProt GroupP0A2U4
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Invasin ipaBC [auth P],
D [auth Q]		22Shigella flexneriMutation(s): 0 
UniProt
Find proteins for P18011 (Shigella flexneri)
Explore P18011 
Go to UniProtKB:  P18011
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP18011
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.201 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.31α = 90
b = 97.09β = 90
c = 106.53γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction
XDSdata scaling
XDSdata reduction

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-06-16
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2021-01-27
    Changes: Data collection, Derived calculations, Source and taxonomy
  • Version 1.3: 2021-11-10
    Changes: Database references
  • Version 1.4: 2023-11-01
    Changes: Data collection, Refinement description