2BL7

1.6 Angstrom crystal structure of EntA-im: a bacterial immunity protein conferring immunity to the antimicrobial activity of the pediocin-like bacteriocin, enterocin A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.210 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

1.6-A Crystal Structure of Enta-Im: A Bacterial Immunity Protein Conferring Immunity to the Antimicrobial Activity of the Pediocin-Like Bacteriocin Enterocin A

Johnsen, L.Dalhus, B.Leiros, I.Nissen-Meyer, J.

(2005) J Biol Chem 280: 19045

  • DOI: https://doi.org/10.1074/jbc.M501386200
  • Primary Citation of Related Structures:  
    2BL7, 2BL8

  • PubMed Abstract: 

    Many Gram-positive bacteria produce ribosomally synthesized antimicrobial peptides, often termed bacteriocins. Genes encoding pediocin-like bacteriocins are generally cotranscribed with or in close vicinity to a gene encoding a cognate immunity protein that protects the bacteriocin-producer from their own bacteriocin. We present the first crystal structure of a pediocin-like immunity protein, EntA-im, conferring immunity to the bacteriocin enterocin A. Determination of the structure of this 103-amino acid protein revealed that it folds into an antiparallel four-helix bundle with a flexible C-terminal part. The fact that the immunity protein conferring immunity to carnobacteriocin B2 also consists of a four-helix bundle (Sprules, T., Kawulka, K. E., and Vederas, J. C. (2004) Biochemistry 43, 11740-11749) strongly indicates that this is a conserved structural motif in all pediocin-like immunity proteins. The C-terminal half of the immunity protein contains a region that recognizes the C-terminal half of the cognate bacteriocin, and the flexibility in the C-terminal end of the immunity protein might thus be an important characteristic that enables the immunity protein to interact with its cognate bacteriocin. By homology modeling of three other pediocin-like immunity proteins and calculation of the surface charge distribution for EntA-im and the three structure models, different charge distributions were observed. The differences in the latter part of helix 3, the beginning of helix 4, and the loop connecting these helices might also be of importance in determining the specificity.


  • Organizational Affiliation

    Program for Biochemistry and Molecular Biology, Department of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway. line.johnsen@biokjemi.uio.no


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ENTEROCINE A IMMUNITY PROTEIN103Enterococcus faeciumMutation(s): 2 
UniProt
Find proteins for Q47785 (Enterococcus faecium)
Explore Q47785 
Go to UniProtKB:  Q47785
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ47785
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.210 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 75.8α = 90
b = 75.8β = 90
c = 36.59γ = 120
Software Package:
Software NamePurpose
CNSrefinement
MOSFLMdata reduction
SCALEITdata scaling
SOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-03-07
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance