5ZCE

Crystal structure of Alpha-glucosidase in complex with maltotetraose

Summary for 5ZCE

• Entry DOI: 10.2210/pdb5zce/pdb
• Related: 5ZCB 5ZCC 5ZCD
• Related PRD ID: PRD_900010
• Descriptor: Alpha-glucosidase, alpha-D-glucopyranose-(1-4)-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: 65715.26

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

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: 29870070
DOI: 10.1002/1873-3468.13126

Experimental method

X-RAY DIFFRACTION (1.555 Å)