2XXP

A widespread family of bacterial cell wall assembly proteins


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.69 Å
  • R-Value Free: 0.224 
  • R-Value Work: 0.189 
  • R-Value Observed: 0.191 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

A Widespread Family of Bacterial Cell Wall Assembly Proteins.

Kawai, Y.Marles-Wright, J.Cleverley, R.M.Emmins, R.Ishikawa, S.Kuwano, M.Heinz, N.Bui, N.K.Hoyland, C.N.Ogasawara, N.Lewis, R.J.Vollmer, W.Daniel, R.A.Errington, J.

(2011) EMBO J 30: 4931

  • DOI: https://doi.org/10.1038/emboj.2011.358
  • Primary Citation of Related Structures:  
    2XXP, 2XXQ, 3TEL, 3TEP, 3TFL

  • PubMed Abstract: 

    Teichoic acids and acidic capsular polysaccharides are major anionic cell wall polymers (APs) in many bacteria, with various critical cell functions, including maintenance of cell shape and structural integrity, charge and cation homeostasis, and multiple aspects of pathogenesis. We have identified the widespread LytR-Cps2A-Psr (LCP) protein family, of previously unknown function, as novel enzymes required for AP synthesis. Structural and biochemical analysis of several LCP proteins suggest that they carry out the final step of transferring APs from their lipid-linked precursor to cell wall peptidoglycan (PG). In Bacillus subtilis, LCP proteins are found in association with the MreB cytoskeleton, suggesting that MreB proteins coordinate the insertion of the major polymers, PG and AP, into the cell wall.


  • Organizational Affiliation

    Centre for Bacterial Cell Biology, Medical School, Newcastle University, Newcastle upon Tyne, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CPS2A398Streptococcus pneumoniae D39Mutation(s): 0 
UniProt
Find proteins for Q9ZII9 (Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466))
Explore Q9ZII9 
Go to UniProtKB:  Q9ZII9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9ZII9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.69 Å
  • R-Value Free: 0.224 
  • R-Value Work: 0.189 
  • R-Value Observed: 0.191 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.56α = 90
b = 73.56β = 90
c = 163.48γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
MOSFLMdata reduction
SCALAdata scaling
SHELXphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2011-10-19
    Type: Initial release
  • Version 1.1: 2011-12-28
    Changes: Other
  • Version 1.2: 2014-01-15
    Changes: Atomic model, Derived calculations, Other