1rzu

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PDB ID 1rzu

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands:
Gene: GLGA1, GLGA, ATU4075, AGR_L_1562 (Agrobacterium tumefaciens)
Activity: Starch synthase, with EC number 2.4.1.21
Related: 1rzv


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the glycogen synthase from A. tumefaciens in complex with ADP


Overview

Glycogen and starch are the major readily accessible energy storage compounds in nearly all living organisms. Glycogen is a very large branched glucose homopolymer containing about 90% alpha-1,4-glucosidic linkages and 10% alpha-1,6 linkages. Its synthesis and degradation constitute central pathways in the metabolism of living cells regulating a global carbon/energy buffer compartment. Glycogen biosynthesis involves the action of several enzymes among which glycogen synthase catalyzes the synthesis of the alpha-1,4-glucose backbone. We now report the first crystal structure of glycogen synthase in the presence and absence of adenosine diphosphate. The overall fold and the active site architecture of the protein are remarkably similar to those of glycogen phosphorylase, indicating a common catalytic mechanism and comparable substrate-binding properties. In contrast to glycogen phosphorylase, glycogen synthase has a much wider catalytic cleft, which is predicted to undergo an important interdomain 'closure' movement during the catalytic cycle. The structures also provide useful hints to shed light on the allosteric regulation mechanisms of yeast/mammalian glycogen synthases.

About this Structure

1RZU is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.

Reference

Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation., Buschiazzo A, Ugalde JE, Guerin ME, Shepard W, Ugalde RA, Alzari PM, EMBO J. 2004 Aug 18;23(16):3196-205. Epub 2004 Jul 22. PMID:15272305

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