|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|
|Date Published||OCT 14|
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.