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7L1Z

Unlocking the structural features for the exo-xylobiosidase activity of an unusual GH11 member identified in a compost-derived consortium - NT-truncated form

7L1Z の概要
エントリーDOI10.2210/pdb7l1z/pdb
分子名称Exo-B-1,4-beta-xylanase, 1,2-ETHANEDIOL, SULFATE ION, ... (4 entities in total)
機能のキーワードglycoside hydrolase family 11, gh11, exo-b-1, 4-xylobiosidase, hydrolase
由来する生物種unidentified
タンパク質・核酸の鎖数3
化学式量合計76410.33
構造登録者
Kadowaki, M.A.S.,Polikarpov, I.,Briganti, L.,Evangelista, D.E. (登録日: 2020-12-15, 公開日: 2021-08-04, 最終更新日: 2023-10-18)
主引用文献Kadowaki, M.A.S.,Briganti, L.,Evangelista, D.E.,Echevarria-Poza, A.,Tryfona, T.,Pellegrini, V.O.A.,Nakayama, D.G.,Dupree, P.,Polikarpov, I.
Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium.
Biotechnol.Bioeng., 118:4052-4064, 2021
Cited by
PubMed Abstract: The heteropolysaccharide xylan is a valuable source of sustainable chemicals and materials from renewable biomass sources. A complete hydrolysis of this major hemicellulose component requires a diverse set of enzymes including endo-β-1,4-xylanases, β-xylosidases, acetylxylan esterases, α-l-arabinofuranosidases, and α-glucuronidases. Notably, the most studied xylanases from glycoside hydrolase family 11 (GH11) have exclusively been endo-β-1,4- and β-1,3-xylanases. However, a recent analysis of a metatranscriptome library from a microbial lignocellulose community revealed GH11 enzymes capable of releasing solely xylobiose from xylan. Although initial biochemical studies clearly indicated their xylobiohydrolase mode of action, the structural features that drive this new activity still remained unclear. It was also not clear whether the enzymes acted on the reducing or nonreducing end of the substrate. Here, we solved the crystal structure of MetXyn11 in the apo and xylobiose-bound forms. The structure of MetXyn11 revealed the molecular features that explain the observed pattern on xylooligosaccharides released by this nonreducing end xylobiohydrolase.
PubMed: 34232504
DOI: 10.1002/bit.27880
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.05 Å)
構造検証レポート
Validation report summary of 7l1z
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-23に公開中

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