4g29

Structure of the Catalytic Domain of the Salmonella Virulence Factor SseI

spinqualitylabelsall models 4g29, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4g29 is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SSEI_SALTY Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is required to maintain a long-term chronic systemic infection in mice. It inhibits normal cell migration of primary macrophages and dendritic cells, by a mechanism that involves interaction with the host factor IQGAP1, an important regulator of the cytoskeleton and cell migration. Also accelerates the systemic spread of infection from the gastrointestinal tract to the bloodstream, probably by interacting with host TRIP6. Publication Abstract from PubMed SseI is secreted into host cells by Salmonella and contributes to the establishment of systemic infections. The crystal structure of the C-terminal domain of SseI has been solved to 1.70 A resolution, revealing it to be a member of the cysteine protease superfamily with a catalytic triad consisting of Cys178, His216 and Asp231 that is critical to its virulence activities. Structure-based analysis revealed that SseI is likely to possess either acyl hydrolase or acyltransferase activity, placing this virulence factor in the rapidly growing class of enzymes of this family utilized by bacterial pathogens inside eukaryotic cells. Structure of the catalytic domain of the Salmonella virulence factor SseI.,Bhaskaran SS, Stebbins CE Acta Crystallogr D Biol Crystallogr. 2012 Dec;68(Pt 12):1613-21. doi:, 10.1107/S0907444912039042. Epub 2012 Nov 9. PMID:23151626 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA