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Catalytic domain of GH30 xylanase C from Talaromyces cellulolyticus
Structural highlights
Publication Abstract from PubMedGH30-7 endoxylanase C from the cellulolytic fungus Talaromyces cellulolyticus (TcXyn30C) belongs to glycoside hydrolase family 30 subfamily 7, and specifically releases 2(2)-(4-O-methyl-alpha-D-glucuronosyl)-xylobiose from glucuronoxylan, as well as various arabino-xylooligosaccharides from arabinoxylan. TcXyn30C has a modular structure consisting of a catalytic domain and a C-terminal cellulose-binding module 1 (CBM1). In this study, the crystal structure of a TcXyn30C mutant which lacks the CBM1 domain was determined at 1.65 A resolution. The structure of the active site of TcXyn30C was compared with that of the bifunctional GH30-7 xylanase B from T. cellulolyticus (TcXyn30B), which exhibits glucuronoxylanase and xylobiohydrolase activities. The results revealed that TcXyn30C has a conserved structural feature for recognizing the 4-O-methyl-alpha-D-glucuronic acid (MeGlcA) substituent in subsite -2b. Additionally, the results demonstrated that Phe47 contributes significantly to catalysis by TcXyn30C. Phe47 is located in subsite -2b and also near the C-3 hydroxyl group of a xylose residue in subsite -2a. Substitution of Phe47 with an arginine residue caused a remarkable decrease in the catalytic efficiency towards arabinoxylan, suggesting the importance of Phe47 in arabinoxylan hydrolysis. These findings indicate that subsite -2b of TcXyn30C has unique structural features that interact with arabinofuranose and MeGlcA substituents. Crystal structure of GH30-7 endoxylanase C from the filamentous fungus Talaromyces cellulolyticus.,Nakamichi Y, Fujii T, Watanabe M, Matsushika A, Inoue H Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):341-349. doi:, 10.1107/S2053230X20009024. Epub 2020 Jul 28. PMID:32744245[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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