PDBsum entry 2wnw

Hydrolase

PDB id: 2wnw

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

Protein chains

Q9KIJ7  (Q9KIJ7_SALTM) -  Glucan endo-1,6-beta-glucosidase from Salmonella typhimurium

Seq: 447 a.a.

Struc: 446 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.75 - glucan endo-1,6-beta-glucosidase.
• Reaction: Random hydrolysis of 1,6-linkages in 1,6-beta-D-glucans.

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.