1gz5
From Proteopedia
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TREHALOSE-6-PHOSPHATE SYNTHASE. OTSA
Overview
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, beta/alpha/beta 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.
About this Structure
1GZ5 is a Single protein structure of sequence from Escherichia coli with G6P, UDP and IMD as ligands. Active as Alpha,alpha-trehalose-phosphate synthase (UDP-forming), with EC number 2.4.1.15 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA., Gibson RP, Turkenburg JP, Charnock SJ, Lloyd R, Davies GJ, Chem Biol. 2002 Dec;9(12):1337-46. PMID:12498887
Page seeded by OCA on Tue Dec 18 15:46:43 2007
