3cx4

Crystal Structure of E.coli GS mutant E377A in complex with ADP and oligosaccharides

spinqualitylabelsall models 3cx4, resolution 2.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3cx4 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.29Å Ligands: 250, ADP, BGC, ETE, GLC, NA, PRD_900001, PRD_900009, PRD_900030 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLGA_ECOLI 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/starch synthase elongates glucan chains and is the key enzyme in the synthesis of glycogen in bacteria and starch in plants. Cocrystallization of Escherichia coli wild-type glycogen synthase (GS) with substrate ADPGlc and the glucan acceptor mimic HEPPSO produced a closed form of GS and suggests that domain-domain closure accompanies glycogen synthesis. Cocrystallization of the inactive GS mutant E377A with substrate ADPGlc and oligosaccharide results in the first oligosaccharide-bound glycogen synthase structure. Four bound oligosaccharides are observed, one in the interdomain cleft (G6a) and three on the N-terminal domain surface (G6b, G6c, and G6d). Extending from the center of the enzyme to the interdomain cleft opening, G6a mostly interacts with the highly conserved N-terminal domain residues lining the cleft of GS. The surface-bound oligosaccharides G6c and G6d have less interaction with enzyme and exhibit a more curled, helixlike structural arrangement. The observation that oligosaccharides bind only to the N-terminal domain of GS suggests that glycogen in vivo probably binds to only one side of the enzyme to ensure unencumbered interdomain movement, which is required for efficient, continuous glucan-chain synthesis. Oligosaccharide binding in Escherichia coli glycogen synthase.,Sheng F, Yep A, Feng L, Preiss J, Geiger JH Biochemistry. 2009 Oct 27;48(42):10089-97. PMID:19761218 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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