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PDBsum entry 2wnw

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2wnw
Jmol
Contents
Protein chains
446 a.a. *
Ligands
PO4 ×4
GOL ×4
Waters ×364
* Residue conservation analysis
PDB id:
2wnw
Name: Hydrolase
Title: The crystal structure of srfj from salmonella typhimurium
Structure: Activated by transcription factor ssrb. Chain: a, b. Synonym: srfj, o-glycosyl hydrolase family 30
Source: Salmonella enterica subsp. Enterica serovar typhimurium str. Lt2. Organism_taxid: 99287
Resolution:
2.00Å     R-factor:   0.199     R-free:   0.215
Authors: Y.-G.Kim,J.-H.Kim,K.-J.Kim
Key ref: Y.G.Kim et al. (2009). Crystal structure of the Salmonella enterica serovar typhimurium virulence factor SrfJ, a glycoside hydrolase family enzyme. J Bacteriol, 191, 6550-6554. PubMed id: 19717598
Date:
20-Jul-09     Release date:   02-Mar-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9KIJ7  (Q9KIJ7_SALTM) -  Lysosomal glucosyl ceramidase
Seq:
Struc:
447 a.a.
446 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   2 terms 
  Biochemical function     glucosylceramidase activity     1 term  

 

 
J Bacteriol 191:6550-6554 (2009)
PubMed id: 19717598  
 
 
Crystal structure of the Salmonella enterica serovar typhimurium virulence factor SrfJ, a glycoside hydrolase family enzyme.
Y.G.Kim, J.H.Kim, K.J.Kim.
 
  ABSTRACT  
 
To cause infection, Salmonella enterica serovar Typhimurium uses type III secretion systems, which are encoded on two Salmonella pathogenicity islands, SPI-1 and SPI-2, the latter of which is thought to play a crucial role in bacterial proliferation in Salmonella-containing vacuoles (SCVs) after invading cells. S. Typhimurium SrfJ, located outside SPI-2, is also known to be involved in Salmonella pathogenicity and has high amino acid sequence homology with human lysosomal glucosylceramidase (GlcCerase). We present the first crystal structure of SrfJ at a resolution of 1.8 A. The overall fold of SrfJ shares high structure similarities with that of human GlcCerase, comprising two distinctive domains: a (beta/alpha)(8)-barrel catalytic domain and a beta-sandwich domain. As in human GlcCerase, the pocket-shaped active site of SrfJ is located on the C-terminal side of the barrel, and two conserved glutamic acid residues are used for the enzyme catalysis. Moreover, a glycerol-bound form of SrfJ reveals that the glucose ring moiety of the substrate might similarly bind to the enzyme as to human GlcCerase, suggesting that SrfJ might function as a glycoside hydrolase. Although some structural differences are observed between SrfJ and human GlcCerase in the substrate entrance of the active site, we speculate that, based on the high structural similarities to human GlcCerase in the overall fold and the active-site environment, SrfJ might have a GlcCerase activity and use the activity to enhance Salmonella virulence by modifying SCV membrane lipids.