2QZS
Crystal Structure of Wild-type E.coli GS in complex with ADP and Glucose(wtGSb)
Summary for 2QZS
| Entry DOI | 10.2210/pdb2qzs/pdb |
| Related | 2QYY |
| Descriptor | glycogen synthase, alpha-D-glucopyranose, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | glycosyl-transferase, gt-b fold, rossmann fold, closed-form, adp and glucose binding, glycogen biosynthesis, glycosyltransferase, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 54827.04 |
| Authors | Sheng, F.,Geiger, J. (deposition date: 2007-08-17, 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 Cited by 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: 19244233DOI: 10.1074/jbc.M809804200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
