Title | Structural and Kinetic Analysis of Substrate Binding to the Sialyltransferase Cst-II from Campylobacter jejuni |
Publication Type | Journal Article |
Year of Publication | 2011 |
Authors | Lee, HJun, Lairson, LL, Rich, JR, Lameignere, E, Wakarchuk, WW, Withers, SG, Strynadka, NCJ |
Journal | JOURNAL OF BIOLOGICAL CHEMISTRY |
Volume | 286 |
Pagination | 35922-35932 |
Date Published | OCT 14 |
ISSN | 0021-9258 |
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. |
DOI | 10.1074/jbc.M111.261172 |