1GKL
S954A mutant of the feruloyl esterase module from clostridium thermocellum complexed with ferulic acid
1GKL の概要
| エントリーDOI | 10.2210/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: 11738044DOI: 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) |
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