3IK2

Crystal Structure of a Glycoside Hydrolase Family 44 Endoglucanase produced by Clostridium acetobutylium ATCC 824

3IK2 の概要

• エントリーDOI: 10.2210/pdb3ik2/pdb
• 分子名称: Endoglucanase A, CHLORIDE ION, CALCIUM ION, ... (7 entities in total)
• 機能のキーワード: tim-like barrel, hydrolase
• 由来する生物種: Clostridium acetobutylicum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58890.57

構造登録者

Warner, C.D.,Hoy, J.A.,Ford, C.F.,Honzatko, R.B.,Reilly, P.J. (登録日: 2009-08-05, 公開日: 2009-08-18, 最終更新日: 2023-09-06)

主引用文献

Warner, C.D.,Hoy, J.A.,Shilling, T.C.,Linnen, M.J.,Ginder, N.D.,Ford, C.F.,Honzatko, R.B.,Reilly, P.J.
Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from Clostridium acetobutylicum.
Appl.Environ.Microbiol., 76:338-346, 2010

PubMed Abstract: A gene encoding a glycoside hydrolase family 44 (GH44) protein from Clostridium acetobutylicum ATCC 824 was synthesized and transformed into Escherichia coli. The previously uncharacterized protein was expressed with a C-terminal His tag and purified by nickel-nitrilotriacetic acid affinity chromatography. Crystallization and X-ray diffraction to a 2.2-A resolution revealed a triose phosphate isomerase (TIM) barrel-like structure with additional Greek key and beta-sandwich folds, similar to other GH44 crystal structures. The enzyme hydrolyzes cellotetraose and larger cellooligosaccharides, yielding an unbalanced product distribution, including some glucose. It attacks carboxymethylcellulose and xylan at approximately the same rates. Its activity on carboxymethylcellulose is much higher than that of the isolated C. acetobutylicum cellulosome. It also extensively converts lichenan to oligosaccharides of intermediate size and attacks Avicel to a limited extent. The enzyme has an optimal temperature in a 10-min assay of 55 degrees C and an optimal pH of 5.0.

PubMed: 19915043
DOI: 10.1128/AEM.02026-09

実験手法

X-RAY DIFFRACTION (2.2 Å)