2E0P
The crystal structure of Cel44A
2E0P の概要
エントリーDOI | 10.2210/pdb2e0p/pdb |
関連するBIRD辞書のPRD_ID | PRD_900011 |
分子名称 | Endoglucanase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, GLYCEROL, ... (7 entities in total) |
機能のキーワード | tim-like barrel, tim barrel, the composite domain of gh family 5, 30, 39, 51, structural genomics, hydrolase |
由来する生物種 | Clostridium thermocellum |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 58772.32 |
構造登録者 | Kitago, Y.,Karita, S.,Watanabe, N.,Sakka, K.,Tanaka, I. (登録日: 2006-10-11, 公開日: 2007-09-18, 最終更新日: 2023-10-25) |
主引用文献 | Kitago, Y.,Karita, S.,Watanabe, N.,Kamiya, M.,Aizawa, T.,Sakka, K.,Tanaka, I. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J.Biol.Chem., 282:35703-35711, 2007 Cited by PubMed Abstract: The crystal structure of Cel44A, which is one of the enzymatic components of the cellulosome of Clostridium thermocellum, was solved at a resolution of 0.96 A. This enzyme belongs to glycoside hydrolase family (GH family) 44. The structure reveals that Cel44A consists of a TIM-like barrel domain and a beta-sandwich domain. The wild-type and the E186Q mutant structures complexed with substrates suggest that two glutamic acid residues, Glu(186) and Glu(359), are the active residues of the enzyme. Biochemical experiments were performed to confirm this idea. The structural features indicate that GH family 44 belongs to clan GH-A and that the reaction catalyzed by Cel44A is retaining type hydrolysis. The stereochemical course of hydrolysis was confirmed by a (1)H NMR experiment using the reduced cellooligosaccharide as a substrate. PubMed: 17905739DOI: 10.1074/jbc.M706835200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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