6HS6

C-terminal domain of the TssA component of the type VI secretion system from Burkholderia cenocepacia


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.08 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.200 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structural insights into the function of type VI secretion system TssA subunits.

Dix, S.R.Owen, H.J.Sun, R.Ahmad, A.Shastri, S.Spiewak, H.L.Mosby, D.J.Harris, M.J.Batters, S.L.Brooker, T.A.Tzokov, S.B.Sedelnikova, S.E.Baker, P.J.Bullough, P.A.Rice, D.W.Thomas, M.S.

(2018) Nat Commun 9: 4765-4765

  • DOI: https://doi.org/10.1038/s41467-018-07247-1
  • Primary Citation of Related Structures:  
    6G7B, 6G7C, 6H8E, 6H8F, 6HS5, 6HS6

  • PubMed Abstract: 

    The type VI secretion system (T6SS) is a multi-protein complex that injects bacterial effector proteins into target cells. It is composed of a cell membrane complex anchored to a contractile bacteriophage tail-like apparatus consisting of a sharpened tube that is ejected by the contraction of a sheath against a baseplate. We present structural and biochemical studies on TssA subunits from two different T6SSs that reveal radically different quaternary structures in comparison to the dodecameric E. coli TssA that arise from differences in their C-terminal sequences. Despite this, the different TssAs retain equivalent interactions with other components of the complex and position their highly conserved N-terminal ImpA_N domain at the same radius from the centre of the sheath as a result of their distinct domain architectures, which includes additional spacer domains and highly mobile interdomain linkers. Together, these variations allow these distinct TssAs to perform a similar function in the complex.


  • Organizational Affiliation

    Department of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Sheffield, S10 2TN, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Type VI secretion protein ImpA75Burkholderia cenocepacia H111Mutation(s): 0 
Gene Names: I35_RS01755
UniProt
Find proteins for A0A1V2W6E8 (Burkholderia cenocepacia)
Explore A0A1V2W6E8 
Go to UniProtKB:  A0A1V2W6E8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A1V2W6E8
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.08 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.200 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.33α = 90
b = 201.7β = 90
c = 263.66γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
xia2data reduction
xia2data scaling
SHELXCDphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Biotechnology and Biological Sciences Research CouncilUnited KingdomBB/J014443/1
Biotechnology and Biological Sciences Research CouncilUnited KingdomBB/F016840/1
Higher Education Funding Council for EnglandUnited KingdomR/151699

Revision History  (Full details and data files)

  • Version 1.0: 2018-11-21
    Type: Initial release
  • Version 1.1: 2024-05-15
    Changes: Data collection, Database references