7d9c | pdb_00007d9c

Alpha-glucosidase from Weissella cibaria BBK-1 bound with maltose

spinqualitylabelsall models 7d9c, resolution 1.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7d9c is a 1 chain structure with sequence from Weissella confusa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.36Å Ligands: BGC, CA, GLC, MES, PRD_900001, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A482PRE5_WEICO Publication Abstract from PubMed alpha-Glucosidase (EC 3.2.1.20) is a carbohydrate-hydrolyzing enzyme which generally cleaves alpha-1,4-glycosidic bonds of oligosaccharides and starch from the nonreducing ends. In this study, the novel alpha-glucosidase from Weissella cibaria BBK-1 (WcAG) was biochemically and structurally characterized. WcAG belongs to glycoside hydrolase family 13 (GH13) and to the neopullanase subfamily. It exhibits distinct hydrolytic activity towards the alpha-1,4 linkages of short-chain oligosaccharides from the reducing end. The enzyme prefers to hydrolyse maltotriose and acarbose, while it cannot hydrolyse cyclic oligosaccharides and polysaccharides. In addition, WcAG can cleave pullulan hydrolysates and strongly exhibits transglycosylation activity in the presence of maltose. Size-exclusion chromatography and X-ray crystal structures revealed that WcAG forms a homodimer in which the N-terminal domain of one monomer is orientated in proximity to the catalytic domain of another, creating the substrate-binding groove. Crystal structures of WcAG in complexes with maltose, maltotriose and acarbose revealed a remarkable enzyme active site with accessible +2, +1 and -1 subsites, along with an Arg-Glu gate (Arg176-Glu296) in front of the active site. The -2 and -3 subsites were blocked by Met119 and Asn120 from the N-terminal domain of a different subunit, resulting in an extremely restricted substrate preference. A GH13 alpha-glucosidase from Weissella cibaria uncommonly acts on short-chain maltooligosaccharides.,Wangpaiboon K, Laohawuttichai P, Kim SY, Mori T, Nakapong S, Pichyangkura R, Pongsawasdi P, Hakoshima T, Krusong K Acta Crystallogr D Struct Biol. 2021 Aug 1;77(Pt 8):1064-1076. doi:, 10.1107/S205979832100677X. Epub 2021 Jul 29. PMID:34342279 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alpha-glucosidase 3D structures

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