5zce | pdb_00005zce

Crystal structure of Alpha-glucosidase in complex with maltotetraose

spinqualitylabelsall models 5zce, resolution 1.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zce is a 1 chain structure with sequence from Bacillus sp. (in: Bacteria). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.555Å Ligands: CA, GLC, PRD_900010 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2Z5WH92_BACSP Publication Abstract from PubMed alpha-Glucosidase hydrolyzes alpha-glucosides and transfers alpha-glucosyl residues to an acceptor through transglucosylation. In this study, GH13_31 alpha-glucosidase BspAG13_31A with high transglucosylation activity is reported in Bacillus sp. AHU2216 and biochemically and structurally characterized. This enzyme is specific to alpha-(1-->4)-glucosidic linkage as substrates and transglucosylation products. Maltose is the most preferred substrate. Crystal structures of BspAG13_31A wild-type for the substrate-free form and inactive acid/base mutant E256Q in complexes with maltooligosaccharides were solved at 1.6-2.5 A resolution. BspAG13_31A has a catalytic domain folded by an (beta/alpha)8 -barrel. In subsite +1, Ala200 and His203 on beta-->alpha loop 4 and Asn258 on beta-->alpha loop 5 are involved in the recognition of maltooligosaccharides. Structural basis for specificity of GH13_31 enzymes to alpha-(1-->4)-glucosidic linkage is first described. Function and structure of GH13_31 alpha-glucosidase with high alpha-(1-->4)-glucosidic linkage specificity and transglucosylation activity.,Auiewiriyanukul W, Saburi W, Kato K, Yao M, Mori H FEBS Lett. 2018 Jul;592(13):2268-2281. doi: 10.1002/1873-3468.13126. Epub 2018, Jun 20. PMID:29870070 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alpha-glucosidase 3D structures

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