2VXY

The structure of FTsZ from Bacillus subtilis at 1.7A resolution


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.186 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

An Inhibitor of Ftsz with Potent and Selective Anti-Staphylococcal Activity.

Haydon, D.J.Stokes, N.R.Ure, R.Galbraith, G.Bennett, J.M.Brown, D.R.Baker, P.J.Barynin, V.V.Rice, D.W.Sedelnikova, S.E.Heal, J.R.Sheridan, J.M.Aiwale, S.T.Chauhan, P.K.Srivastava, A.Taneja, A.Collins, I.Errington, J.Czaplewski, L.G.

(2008) Science 321: 1673

  • DOI: https://doi.org/10.1126/science.1159961
  • Primary Citation of Related Structures:  
    2VXY

  • PubMed Abstract: 

    FtsZ is an essential bacterial guanosine triphosphatase and homolog of mammalian beta-tubulin that polymerizes and assembles into a ring to initiate cell division. We have created a class of small synthetic antibacterials, exemplified by PC190723, which inhibits FtsZ and prevents cell division. PC190723 has potent and selective in vitro bactericidal activity against staphylococci, including methicillin- and multi-drug-resistant Staphylococcus aureus. The putative inhibitor-binding site of PC190723 was mapped to a region of FtsZ that is analogous to the Taxol-binding site of tubulin. PC190723 was efficacious in an in vivo model of infection, curing mice infected with a lethal dose of S. aureus. The data validate FtsZ as a target for antibacterial intervention and identify PC190723 as suitable for optimization into a new anti-staphylococcal therapy.


  • Organizational Affiliation

    Prolysis, Begbroke Science Park, Oxfordshire OX5 1PF, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CELL DIVISION PROTEIN FTSZ382Bacillus subtilisMutation(s): 0 
UniProt
Find proteins for P17865 (Bacillus subtilis (strain 168))
Explore P17865 
Go to UniProtKB:  P17865
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP17865
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.186 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 87.17α = 90
b = 87.17β = 90
c = 89.46γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2008-09-30
    Type: Initial release
  • Version 1.1: 2011-05-07
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description