6KRN
Crystal structure of GH30 xylanase B from Talaromyces cellulolyticus expressed by Pichia pastoris in complex with aldotriuronic acid
6KRN の概要
エントリーDOI | 10.2210/pdb6krn/pdb |
関連するPDBエントリー | 6KRL |
分子名称 | Mating factor alpha,GH30 Xylanase B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
機能のキーワード | xylanase, glucuronoxylanase, hydrolase |
由来する生物種 | Saccharomyces uvarum (Yeast) 詳細 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 63030.66 |
構造登録者 | |
主引用文献 | Nakamichi, Y.,Watanabe, M.,Matsushika, A.,Inoue, H. Substrate recognition by a bifunctional GH30-7 xylanase B from Talaromyces cellulolyticus. Febs Open Bio, 10:1180-1189, 2020 Cited by PubMed Abstract: Xylanase B, a member of subfamily 7 of the GH30 (glycoside hydrolase family 30) from Talaromyces cellulolyticus (TcXyn30B), is a bifunctional enzyme with glucuronoxylanase and xylobiohydrolase activities. In the present study, crystal structures of the native enzyme and the enzyme-product complex of TcXyn30B expressed in Pichia pastoris were determined at resolutions of 1.60 and 1.65 Å, respectively. The enzyme complexed with 2 -(4-O-methyl-α-d-glucuronyl)-xylobiose (U X) revealed that TcXyn30B strictly recognizes both the C-6 carboxyl group and the 4-O-methyl group of the 4-O-methyl-α-d-glucuronyl side chain by the conserved residues in GH30-7 endoxylanases. The crystal structure and site-directed mutagenesis indicated that Asn-93 on the β2-α2-loop interacts with the non-reducing end of the xylose residue at subsite-2 and is likely to be involved in xylobiohydrolase activity. These findings provide structural insight into the mechanisms of substrate recognition of GH30-7 glucuronoxylanase and xylobiohydrolase. PubMed: 32359208DOI: 10.1002/2211-5463.12873 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.653 Å) |
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