2VH2

Crystal structure of cell divison protein FtsQ from Yersinia enterecolitica


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.323 
  • R-Value Work: 0.277 
  • R-Value Observed: 0.277 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structural and Mutational Analysis of Cell Division Protein Ftsq

van den Ent, F.Vinkenvleugel, T.Ind, A.West, P.Veprintsev, D.Naninga, N.den Blaauwen, T.Lowe, J.

(2008) Mol Microbiol 68: 110

  • DOI: https://doi.org/10.1111/j.1365-2958.2008.06141.x
  • Primary Citation of Related Structures:  
    2VH1, 2VH2

  • PubMed Abstract: 

    Bacterial cytokinesis requires the divisome, a complex of proteins that co-ordinates the invagination of the cytoplasmic membrane, inward growth of the peptidoglycan layer and the outer membrane. Assembly of the cell division proteins is tightly regulated and the order of appearance at the future division site is well organized. FtsQ is a highly conserved component of the divisome among bacteria that have a cell wall, where it plays a central role in the assembly of early and late cell division proteins. Here, we describe the crystal structure of the major, periplasmic domain of FtsQ from Escherichia coli and Yersinia enterocolitica. The crystal structure reveals two domains; the alpha-domain has a striking similarity to polypeptide transport-associated (POTRA) domains and the C-terminal beta-domain forms an extended beta-sheet overlaid by two, slightly curved alpha-helices. Mutagenesis experiments demonstrate that two functions of FtsQ, localization and recruitment, occur in two separate domains. Proteins that localize FtsQ need the second beta-strand of the POTRA domain and those that are recruited by FtsQ, like FtsL/FtsB, require the surface formed by the tip of the last alpha-helix and the two C-terminal beta-strands. Both domains act together to accomplish the role of FtsQ in linking upstream and downstream cell division proteins within the divisome.


  • Organizational Affiliation

    MRC-LMB, Hills Road, Cambridge CB2 2QH, UK. fent@mrc-lmb.cam.ac.uk


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CELL DIVISION PROTEIN FTSQ
A, B
255Yersinia enterocoliticaMutation(s): 0 
UniProt
Find proteins for A1JJJ6 (Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081))
Explore A1JJJ6 
Go to UniProtKB:  A1JJJ6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA1JJJ6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.323 
  • R-Value Work: 0.277 
  • R-Value Observed: 0.277 
  • Space Group: P 62
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 160.76α = 90
b = 160.76β = 90
c = 54.575γ = 120
Software Package:
Software NamePurpose
CNSrefinement
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-03-11
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-24
    Changes: Database references, Source and taxonomy
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Other, Refinement description