5ZCD
Crystal structure of Alpha-glucosidase in complex with maltotriose
Summary for 5ZCD
| Entry DOI | 10.2210/pdb5zcd/pdb |
| Related | 5ZCB 5ZCC |
| Related PRD ID | PRD_900009 |
| Descriptor | Alpha-glucosidase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | alpha-glucosidase, hydrolase |
| Biological source | Bacillus sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 65553.12 |
| Authors | Kato, K.,Saburi, W.,Yao, M. (deposition date: 2018-02-16, release date: 2018-12-26, Last modification date: 2023-11-22) |
| Primary citation | Auiewiriyanukul, W.,Saburi, W.,Kato, K.,Yao, M.,Mori, H. Function and structure of GH13_31 alpha-glucosidase with high alpha-(1→4)-glucosidic linkage specificity and transglucosylation activity. FEBS Lett., 592:2268-2281, 2018 Cited by PubMed Abstract: α-Glucosidase hydrolyzes α-glucosides and transfers α-glucosyl residues to an acceptor through transglucosylation. In this study, GH13_31 α-glucosidase BspAG13_31A with high transglucosylation activity is reported in Bacillus sp. AHU2216 and biochemically and structurally characterized. This enzyme is specific to α-(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 Å resolution. BspAG13_31A has a catalytic domain folded by an (β/α) -barrel. In subsite +1, Ala200 and His203 on β→α loop 4 and Asn258 on β→α loop 5 are involved in the recognition of maltooligosaccharides. Structural basis for specificity of GH13_31 enzymes to α-(1→4)-glucosidic linkage is first described. PubMed: 29870070DOI: 10.1002/1873-3468.13126 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.707 Å) |
Structure validation
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