Browse by author
Lookup NU author(s): Dr Ruth Lloyd
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Trehalose is a nonreducing disaccharide that plays a major role in many organisms, most notably in survival and stress responses. In Mycobacterium tuberculosis, it plays a central role as the carbohydrate core of numerous immunogenic glycolipids including "cord factor" (trehalose 6,6′-dimycolate). The classical pathway for trehalose synthesis involves the condensation of UDP-glucose and glucose-6-phosphate to afford trehalose-6-phosphate, catalyzed by the retaining glycosyltransferase OtsA. The configurations of two anomeric positions are set simultaneously, resulting in the formation of a double glycoside. The three-dimensional structure of the Escherichia coli OtsA, in complex with both UDP and glucose-6-phosphate, reveals the active site at the interface of two β/α/β domains. The overall structure and the intimate details of the catalytic machinery reveal a striking similarity to glycogen phosphorylase, indicating a strong evolutionary link and suggesting a common catalytic mechanism.
Author(s): Gibson RP, Turkenburg JP, Charnock SJ, Lloyd R, Davies GJ
Publication type: Article
Publication status: Published
Journal: Chemistry and Biology
Year: 2002
Volume: 9
Issue: 12
Pages: 1337-1346
ISSN (print): 1074-5521
ISSN (electronic): 1879-1301
Publisher: Cell Press
URL: http://dx.doi.org/10.1016/S1074-5521(02)00292-2
DOI: 10.1016/S1074-5521(02)00292-2
PubMed id: 12498887
Altmetrics provided by Altmetric
