1gz5
From Proteopedia
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| , resolution 2.43Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Alpha,alpha-trehalose-phosphate synthase (UDP-forming), with EC number 2.4.1.15 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 20:54:23 2008
