1rzu

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

spinqualitylabelsall models 1rzu, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1rzu is a 2 chain structure with sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: ADP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLGA1_RHIRD Synthesizes alpha-1,4-glucan chains using ADP-glucose. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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