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PDBsum entry 2fu2

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protein links
Structural genomics, unknown function PDB id
2fu2

 

 

 

 

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Contents
Protein chain
78 a.a. *
Waters ×67
* Residue conservation analysis
PDB id:
2fu2
Name: Structural genomics, unknown function
Title: Crystal structure of protein spy2152 from streptococcus pyogenes
Structure: Hypothetical protein spy2152. Chain: a. Engineered: yes
Source: Streptococcus pyogenes. Organism_taxid: 1314. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.15Å     R-factor:   0.161     R-free:   0.254
Authors: C.Chang,M.Cymborowski,Z.Otwinowski,W.Minor,L.-E.Lezondra,S.Clancy, A.Joachimiak,Midwest Center For Structural Genomics (Mcsg)
Key ref: C.Chang et al. (2009). The structure of pyogenecin immunity protein, a novel bacteriocin-like immunity protein from Streptococcus pyogenes. Bmc Struct Biol, 9, 75-75. PubMed id: 20017931
Date:
25-Jan-06     Release date:   07-Mar-06    
PROCHECK
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 Headers
 References

Protein chain
Q48QT2  (Q48QT2_STRPM) -  Bacteriocin from Streptococcus pyogenes serotype M28 (strain MGAS6180)
Seq:
Struc:
108 a.a.
78 a.a.
Key:    Secondary structure  CATH domain

 

 
Bmc Struct Biol 9:75-75 (2009)
PubMed id: 20017931  
 
 
The structure of pyogenecin immunity protein, a novel bacteriocin-like immunity protein from Streptococcus pyogenes.
C.Chang, P.Coggill, A.Bateman, R.D.Finn, M.Cymborowski, Z.Otwinowski, W.Minor, L.Volkart, A.Joachimiak.
 
  ABSTRACT  
 
BACKGROUND: Many Gram-positive lactic acid bacteria (LAB) produce anti-bacterial peptides and small proteins called bacteriocins, which enable them to compete against other bacteria in the environment. These peptides fall structurally into three different classes, I, II, III, with class IIa being pediocin-like single entities and class IIb being two-peptide bacteriocins. Self-protective cognate immunity proteins are usually co-transcribed with these toxins. Several examples of cognates for IIa have already been solved structurally. Streptococcus pyogenes, closely related to LAB, is one of the most common human pathogens, so knowledge of how it competes against other LAB species is likely to prove invaluable. RESULTS: We have solved the crystal structure of the gene-product of locus Spy_2152 from S. pyogenes, (PDB:2fu2), and found it to comprise an anti-parallel four-helix bundle that is structurally similar to other bacteriocin immunity proteins. Sequence analyses indicate this protein to be a possible immunity protein protective against class IIa or IIb bacteriocins. However, given that S. pyogenes appears to lack any IIa pediocin-like proteins but does possess class IIb bacteriocins, we suggest this protein confers immunity to IIb-like peptides. CONCLUSIONS: Combined structural, genomic and proteomic analyses have allowed the identification and in silico characterization of a new putative immunity protein from S. pyogenes, possibly the first structure of an immunity protein protective against potential class IIb two-peptide bacteriocins. We have named the two pairs of putative bacteriocins found in S. pyogenes pyogenecin 1, 2, 3 and 4.
 

 

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