Wednesday, March 9, 2011, 11:00 am — John Dunn Seminar Room, Bldg. 463
Symbiotic colonic bacteria, typified by Bacteroides thetaiotaomicron, play a key role in maintaining human health by harnessing large families of glycoside hydrolases (GHs) to exploit dietary polysaccharides and host glycans as nutrients. Such GH family functional expansion is exemplified by the 23 family GH92 glycosidases encoded by the B. thetaiotaomicron genome. The three-dimensional structures of GH92 mannosidases defines a family of two-domain proteins in which the catalytic center is located at the domain interface, with hydrolysis proceeding in a Ca2+-dependent manner. The three-dimensional structures of Bacteroides GH92s in complex with various inhibitors provide insight into substrate specificity, mechanism and conformational itinerary of catalysis, and will be compared with another mannosidase family, GH38.
Hosted by: Alexei Soares
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