2R4U

Crystal Structure of Wild-type E.coli GS in complex with ADP and Glucose(wtGSd)

Summary for 2R4U

• Entry DOI: 10.2210/pdb2r4u/pdb
• Related: 2QYY 2QZS 2R4T
• Descriptor: Glycogen synthase, alpha-D-glucopyranose, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: glycosyl-transferase, gt-b fold, rossmann fold, closed-form, adp and glucose binding, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 56731.29

Authors

Sheng, F.,Geiger, J. (deposition date: 2007-09-01, release date: 2008-09-09, Last modification date: 2023-08-30)

Primary citation

Sheng, F.,Jia, X.,Yep, A.,Preiss, J.,Geiger, J.H.
The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase.
J.Biol.Chem., 284:17796-17807, 2009

PubMed 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.

PubMed: 19244233
DOI: 10.1074/jbc.M809804200

Experimental method

X-RAY DIFFRACTION (2.367 Å)