4g29
Structure of the Catalytic Domain of the Salmonella Virulence Factor SseI
Structural highlights
FunctionSSEI_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.[1] [2] Publication Abstract from PubMedSseI 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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