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1GKL

S954A mutant of the feruloyl esterase module from clostridium thermocellum complexed with ferulic acid

1GKL の概要
エントリーDOI10.2210/pdb1gkl/pdb
関連するPDBエントリー1DYO 1GKK 1H6X 1H6Y
分子名称ENDO-1,4-BETA-XYLANASE Y, 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID, GLYCEROL, ... (6 entities in total)
機能のキーワードhydrolase, esterase family 1, inactive mutant
由来する生物種CLOSTRIDIUM THERMOCELLUM
タンパク質・核酸の鎖数2
化学式量合計69720.84
構造登録者
Prates, J.A.M.,Tarbouriech, N.,Charnock, S.J.,Fontes, C.M.G.A.,Ferreira, L.M.A.,Davies, G.J. (登録日: 2001-08-15, 公開日: 2001-12-13, 最終更新日: 2024-05-08)
主引用文献Prates, J.A.,Tarbouriech, N.,Charnock, S.J.,Fontes, C.M.,Ferreira, L.M.,Davies, G.J.
The structure of the feruloyl esterase module of xylanase 10B from Clostridium thermocellum provides insights into substrate recognition.
Structure, 9:1183-1190, 2001
Cited by
PubMed Abstract: Degradation of the plant cell wall requires the synergistic action of a consortium of predominantly modular enzymes. In Clostridiae, these biocatalysts are organized into a supramolecular assembly termed a "cellulosome." This multienzyme complex possesses, in addition to its well-described cellulolytic activity, an apparatus specific for xylan degradation. Cinnamic acid esterases hydrolyze the ferulate groups involved in the crosslinking of arabinoxylans to lignin and thus play a key role in the degradation of the plant cell wall in addition to having promising industrial and medical applications.
PubMed: 11738044
DOI: 10.1016/s0969-2126(01)00684-0
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.4 Å)
構造検証レポート
Validation report summary of 1gkl
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2025-12-31に公開中

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