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Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA

Lookup NU author(s): Dr Ruth Lloyd

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Abstract

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.

Publication metadata

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

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