1gz5

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Davies, G.J.]]
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[[Category: Davies, G J.]]
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[[Category: Gibson, R.P.]]
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[[Category: Gibson, R P.]]
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[[Category: Turkenburg, J.P.]]
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[[Category: Turkenburg, J P.]]
[[Category: G6P]]
[[Category: G6P]]
[[Category: IMD]]
[[Category: IMD]]
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[[Category: trehalose-6-phosphate]]
[[Category: trehalose-6-phosphate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:44:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:37 2008''

Revision as of 10:55, 21 February 2008


1gz5, resolution 2.43Å

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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 , and 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

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