NDLI: The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase.

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The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase.

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The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Geiger, James H. Sheng, Fang Jia, Xiaofei Yep, Alejandra Preiss, Jack
Description	Author Affiliation: Sheng F ( Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA.)
Abstract	Escherichia coli glycogen synthase (EcGS, EC 2.4.1.21) is a retaining glycosyltransferase (GT) that transfers glucose from adenosine diphosphate glucose to a glucan chain acceptor with retention of configuration at the anomeric carbon. EcGS belongs to the GT-B structural superfamily. Here we report several EcGS x-ray structures that together shed considerable light on the structure and function of these enzymes. The structure of the wild-type enzyme bound to ADP and glucose revealed a 15.2 degrees overall domain-domain closure and provided for the first time the structure of the catalytically active, closed conformation of a glycogen synthase. The main chain carbonyl group of His-161, Arg-300, and Lys-305 are suggested by the structure to act as critical catalytic residues in the transglycosylation. Glu-377, previously thought to be catalytic is found on the alpha-face of the glucose and plays an electrostatic role in the active site and as a glucose ring locator. This is also consistent with the structure of the EcGS(E377A)-ADP-HEPPSO complex where the glucose moiety is either absent or disordered in the active site.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	26
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-06-26
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Diphosphate Glucose Metabolism Escherichia Coli Enzymology Glycogen Synthase Chemistry Binding Sites Crystallography, X-Ray Models, Molecular Protein Binding Protein Structure, Tertiary Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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