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Aspergillus sojae alpha-glucosidase AsojAgdL in complex with trehaloseAspergillus sojae alpha-glucosidase AsojAgdL in complex with trehalose
Structural highlights
FunctionA0A5N6EXS6_9EURO Glucosidase involved in the degradation of cellulosic biomass. Has both alpha- and beta-glucosidase activity.[ARBA:ARBA00025512] Publication Abstract from PubMedAn alpha-glucosidase from Aspergillus sojae, AsojAgdL, exhibits strong transglucosylation activity to produce alpha-1,6-glucosidic linkages. The most remarkable structural feature of AsojAgdL is that residues 457-560 of AsojAgdL (designated the NC sequence) is not conserved in other glycoside hydrolase family 31 enzymes, and part of this NC sequence is proteolytically cleaved during its maturation. In this study, the enzyme was expressed in Pichia pastoris, and electrophoretic analysis indicated that the recombinant enzyme, rAsojAgdL, consisted of two polypeptide chains, as observed in the case of the enzyme produced in an Aspergillus strain. The crystal structure of rAsojAgdL was determined in complex with the substrate analog trehalose. Electron density corresponding to residues 496-515 of the NC sequence was not seen, and there were no alpha-helices or beta-strands except for a short alpha-helix in the structures of residues 457-495 and residues 516-560, both of which belong to the NC sequence. The residues 457-495 and the residues 516-560 both formed extra components of the catalytic domain. The residues 457-495 constituted the entrance of the catalytic pocket of rAsojAgdL, and Gly467, Asp468, Pro469, and Pro470 in the NC sequence were located within 4 A of Trp400, a key residue involved in binding of the substrate. The results suggest that the proteolytic processing of the NC sequence is related to the formation of the catalytic pocket of AsojAgdL. Structural basis for proteolytic processing of Aspergillus sojae alpha-glucosidase L with strong transglucosylation activity.,Ding Y, Oyagi A, Miyasaka Y, Kozono T, Sasaki N, Kojima Y, Yoshida M, Matsumoto Y, Yasutake N, Nishikawa A, Tonozuka T J Struct Biol. 2022 Sep;214(3):107874. doi: 10.1016/j.jsb.2022.107874. Epub 2022 , Jun 7. PMID:35688347[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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