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• W197602360 abstract "EpsE is an ATPase that powers transport of cholera toxin and hydrolytic enzymes through the type II secretion (T2S) apparatus in the Gram negative bacterium, Vibrio cholerae. On the basis of structures of homologous Type II/IV secretion ATPases and our biochemical data, we believe that EpsE is active as an oligomer, likely a hexamer, and the binding, hydrolysis and release of nucleotide causes EpsE to undergo dynamic structural changes thus converting chemical energy to mechanical work, ultimately resulting in extracellular secretion. The conformational changes that occur as a consequence of nucleotide binding would realign conserved arginines (R210, R225, R320, R324, R336, and R369) from adjoining domains and subunits to complete the active site around the bound nucleotide. Our data suggests that these arginines are essential for ATP hydrolysis, although their roles in shaping EpsE’s active site are varied. Specifically, we have shown that replacements of these arginine" @default.
• W197602360 created "2016-06-24" @default.
• W197602360 creator A5055821455 @default.
• W197602360 date "2011-01-01" @default.
• W197602360 modified "2023-09-27" @default.
• W197602360 title "Dissecting the Role of EpsE Subdomains in ATPase Activity and Type II Secretion in Vibrio cholerae." @default.
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