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Structural and Kinetic Analysis of Substrate Binding to the Sialyltransferase Cst-II from Campylobacter jejuni

TitleStructural and Kinetic Analysis of Substrate Binding to the Sialyltransferase Cst-II from Campylobacter jejuni
Publication TypeJournal Article
Year of Publication2011
AuthorsLee, HJun, Lairson, LL, Rich, JR, Lameignere, E, Wakarchuk, WW, Withers, SG, Strynadka, NCJ
JournalJOURNAL OF BIOLOGICAL CHEMISTRY
Volume286
Pagination35922-35932
Date PublishedOCT 14
ISSN0021-9258
Abstract

Background: The transfer of sialic acids is catalyzed by a set of sialyltransferases with defined specificities. Results: We solved the ternary complex of the sialyltransferase Cst-II and kinetically characterized its mechanism. Conclusion: Our analysis gives insights into the acceptor specificity and proposes the iso-ordered Bi Bi mechanism. Significance: This work improves our understanding of sialyltransferase structure/function.

DOI10.1074/jbc.M111.261172