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==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.

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==

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[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Davies, G.J.]]

[[Category: Davies, G J.]]

[[Category: Gibson, R.P.]]

[[Category: Gibson, R P.]]

[[Category: Turkenburg, J.P.]]

[[Category: Turkenburg, J P.]]

[[Category: G6P]]

[[Category: IMD]]

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[[Category: trehalose-6-phosphate]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Davies, G.J.]]
+[[Category: Davies, G J.]]
-[[Category: Gibson, R.P.]]
+[[Category: Gibson, R P.]]
-[[Category: Turkenburg, J.P.]]
+[[Category: Turkenburg, J P.]]
 [[Category: G6P]]
 [[Category: IMD]]
@@ Line 27: / Line 27: @@
 [[Category: trehalose-6-phosphate]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:44:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:37 2008''