1GZ1

Mutant D416A of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS in complex with methyl-cellobiosyl-4-deoxy-4-thio-beta-D-cellobioside

1GZ1 の概要

• エントリーDOI: 10.2210/pdb1gz1/pdb
• 関連するPDBエントリー: 1BVW 1HGW 1HGY 1OC5 1OC6 1OC7 1OCB 1OCJ 1OCN 1QJW 1QK0 1QK2 2BVW
• 分子名称: CELLOBIOHYDROLASE II, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-4-thio-beta-D-glucopyranose-(1-4)-methyl beta-D-glucopyranoside, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: hydrolase, cellulose degradation, cellobiohydrolase, cellulase, glycoside hydrolase family 6, thiooligosaccharide
• 由来する生物種: HUMICOLA INSOLENS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40891.33

構造登録者

Varrot, A.,Frandsen, T.,Driguez, H.,Davies, G.J. (登録日: 2002-05-13, 公開日: 2003-02-12, 最終更新日: 2024-10-09)

主引用文献

Varrot, A.,Frandsen, T.,Driguez, H.,Davies, G.J.
Structure of the Humicola Insolens Cellobiohydrolase Cel6A D416A Mutant in Complex with a Non-Hydrolysable Substrate Analogue, Methyl Cellobiosyl-4-Thio-Beta-Cellobioside, at 1.9 A
Acta Crystallogr.,Sect.D, 58:2201-, 2002

PubMed Abstract: The enzymatic degradation of cellulose continues to be one of the most important enzyme-catalysed reactions. Glycoside hydrolases from family GH-6 hydrolyse cellulose with inversion of the configuration of the anomeric carbon. Whilst the catalytic proton donor has been clearly identified (Asp226 in Humicola insolens Cel6A), the identification and even the existence of a potential Brønsted base remains unclear. Equally controversial is the role of surface-loop flexibility. Here, the structure of the D416A mutant of the H. insolens cellobiohydrolase Cel6A in complex with a non-hydrolysable thiooligosaccharide methyl cellobiosyl-4-thio-beta-cellobioside at 1.9 A resolution is presented. Substrate distortion in the -1 subsite, to a (2)S(0) skew-boat conformation, is observed, similar to that seen in the analogous Trichoderma reesei Cel6A structure [Zou et al. (1999), Structure, 7, 1035-1045], but the active-centre N-terminal loop of the H. insolens enzyme is found in a more open conformation than described for previous structures.

PubMed: 12454501
DOI: 10.1107/S0907444902017006

実験手法

X-RAY DIFFRACTION (1.9 Å)