5MXN

Atomic model of the VipA/VipB/Hcp, the type six secretion system non-contractile sheath-tube of Vibrio cholerae from cryo-EM


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.70 Å
  • Aggregation State: HELICAL ARRAY 
  • Reconstruction Method: HELICAL 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Cryo-EM structure of the extended type VI secretion system sheath-tube complex.

Wang, J.Brackmann, M.Castano-Diez, D.Kudryashev, M.Goldie, K.N.Maier, T.Stahlberg, H.Basler, M.

(2017) Nat Microbiol 2: 1507-1512

  • DOI: https://doi.org/10.1038/s41564-017-0020-7
  • Primary Citation of Related Structures:  
    5MXN, 5MYU, 5OJQ

  • PubMed Abstract: 

    The bacterial type VI secretion system (T6SS) uses contraction of a long sheath to quickly thrust a tube with associated effectors across membranes of eukaryotic and bacterial cells 1-5 . Only limited structural information is available about the inherently unstable precontraction state of the T6SS. Here, we obtain a 3.7 Å resolution structure of a non-contractile sheath-tube complex using cryo-electron microscopy and show that it resembles the extended T6SS inside Vibrio cholerae cells. We build a pseudo-atomic model of the complete sheath-tube assembly, which provides a mechanistic understanding of coupling sheath contraction with pushing and rotating the inner tube for efficient target membrane penetration. Our data further show that sheath contraction exposes a buried recognition domain to specifically trigger the disassembly and recycling of the T6SS sheath by the cognate ATP-dependent unfoldase ClpV.


  • Organizational Affiliation

    Focal Area Infection Biology, Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056, Basel, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Haemolysin co-regulated protein170Vibrio choleraeMutation(s): 0 
Gene Names: hcphcpABFX32_16515DA89_871DN30_6EN12_06865EN12_14165
UniProt
Find proteins for P72350 (Vibrio cholerae)
Explore P72350 
Go to UniProtKB:  P72350
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP72350
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Type VI secretion protein473Vibrio choleraeMutation(s): 0 
Gene Names: BFX10_13915BFX32_16935DA89_2095DN30_1329EN12_14575ERS013193_00899
UniProt
Find proteins for Q9KN57 (Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961))
Explore Q9KN57 
Go to UniProtKB:  Q9KN57
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9KN57
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Type VI secretion protein159Vibrio choleraeMutation(s): 0 
Gene Names: BFX10_13910BFX32_16930DA89_2094DN30_1328EN12_14570
UniProt
Find proteins for Q9KN58 (Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961))
Explore Q9KN58 
Go to UniProtKB:  Q9KN58
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9KN58
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.70 Å
  • Aggregation State: HELICAL ARRAY 
  • Reconstruction Method: HELICAL 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION2
MODEL REFINEMENTPHENIX1.11.1-2575

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
SNSFSwitzerland31003A_159525

Revision History  (Full details and data files)

  • Version 1.0: 2017-08-02
    Type: Initial release
  • Version 1.1: 2017-10-11
    Changes: Database references
  • Version 1.2: 2017-11-08
    Changes: Database references