5gr2 | pdb_00005gr2

Crystal structure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142

spinqualitylabelsall models 5gr2, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5gr2 is a 1 chain structure with sequence from Cyaa5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, MG Related: 5gqu, 5gqv, 5gqw, 5gqx, 5gqy, 5gqz, 5gr0, 5gr1, 5gr3, 5gr4, 5gr5, 5gr6 Gene: glgB, glgB1, cce_2248 (CYAA5) Activity: 1,4-alpha-glucan branching enzyme, with EC number 2.4.1.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [B1WPM8_CYAA5] Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.[HAMAP-Rule:MF_00685] Publication Abstract from PubMed Several cyanobacterial species, including Cyanothece sp. ATCC 51142, remarkably have four isoforms of alpha-glucan branching enzymes (BEs). Based on their primary structures, they are classified into glycoside hydrolase (GH) family 13 (BE1, BE2 and BE3) or family 57 (GH57 BE). In the present study, GH13-type BEs from Cyanothece sp. ATCC 51142 (BE1, BE2 and BE3) have been overexpressed in Escherichia coli and biochemically characterized. The recombinant BE1 was crystallized by the hanging-drop vapour-diffusion method. Crystals of BE1 were obtained at 293 K in the presence of 0.2 M Mg(2+), 7-10%(w/v) ethanol, 0.1 M HEPES-NaOH pH 7.2-7.9. The crystals belonged to the tetragonal space group P41212, with unit-cell parameters a = b = 133.75, c = 185.90 A, and diffracted to beyond 1.85 A resolution. Matthews coefficient calculations suggested that the crystals of BE1 contained two molecules in the asymmetric unit. Crystallization and crystallographic analysis of branching enzymes from Cyanothece sp. ATCC 51142.,Hayashi M, Suzuki R, Colleoni C, Ball SG, Fujita N, Suzuki E Acta Crystallogr F Struct Biol Commun. 2015 Aug;71(Pt 8):1109-13. doi:, 10.1107/S2053230X1501198X. Epub 2015 Jul 29. PMID:26249708 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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