8ids | pdb_00008ids

Crystal structure of Bacillus sp. AHU2216 GH13_31 Alpha-glucosidase E256Q/N258P in complex with maltotriose

spinqualitylabelsall models 8ids, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ids 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. Ligands: CA, GLC, PRD_900009 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2Z5WH92_BACSP Publication Abstract from PubMed alpha-Glucosidase catalyzes the hydrolysis of alpha-d-glucosides and transglucosylation. Bacillus sp. AHU2216 alpha-glucosidase (BspAG13_31A), belonging to the glycoside hydrolase family 13 subfamily 31, specifically cleaves alpha-(1-->4)-glucosidic linkages and shows high disaccharide specificity. We showed previously that the maltose moiety of maltotriose (G3) and maltotetraose (G4), covering subsites +1 and +2 of BspAG13_31A, adopts a less stable conformation than the global minimum energy conformation. This unstable d-glucosyl conformation likely arises from steric hindrance by Asn258 on beta-->alpha loop 5 of the catalytic (beta/alpha)(8)-barrel. In this study, Asn258 mutants of BspAG13_31A were enzymatically and structurally analyzed. N258G/P mutations significantly enhanced trisaccharide specificity. The N258P mutation also enhanced the activity toward sucrose and produced erlose from sucrose through transglucosylation. N258G showed a higher specificity to transglucosylation with p-nitrophenyl alpha-d-glucopyranoside and maltose than the wild type. E256Q/N258G and E258Q/N258P structures in complex with G3 revealed that the maltose moiety of G3 bound at subsites +1 and +2 adopted a relaxed conformation, whereas a less stable conformation was taken in E256Q. This structural difference suggests that stabilizing the G3 conformation enhances trisaccharide specificity. The E256Q/N258G-G3 complex formed an additional hydrogen bond between Met229 and the d-glucose residue of G3 in subsite +2, and this interaction may enhance transglucosylation. Alteration of Substrate Specificity and Transglucosylation Activity of GH13_31 alpha-Glucosidase from Bacillus sp. AHU2216 through Site-Directed Mutagenesis of Asn258 on beta-->alpha Loop 5.,Auiewiriyanukul W, Saburi W, Ota T, Yu J, Kato K, Yao M, Mori H Molecules. 2023 Mar 30;28(7):3109. doi: 10.3390/molecules28073109. PMID:37049872 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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