1HF6

ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS IN THE ORTHORHOMBIC CRYSTAL FORM IN COMPLEX WITH CELLOTRIOSE

1HF6 の概要

• エントリーDOI: 10.2210/pdb1hf6/pdb
• 関連するPDBエントリー: 1E5J 1HF5 1HF7 1QHZ 1QI0 1QI2 4A3H 8A3H
• 関連するBIRD辞書のPRD_ID: PRD_900014
• 分子名称: ENDOGLUCANASE B, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: hydrolase, cellulose degradation, endoglucanase, glycoshydrolase family 5
• 由来する生物種: BACILLUS AGARADHAERENS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34842.76

構造登録者

Varrot, A.,Withers, S.,Vasella, A.,Schulein, M.,Davies, G.J. (登録日: 2000-11-29, 公開日: 2001-11-29, 最終更新日: 2023-12-13)

主引用文献

Varrot, A.,Davies, G.J.
Direct Experimental Observation of the Hydrogen-Bonding Network of a Glycosidase Along its Reaction Coordinate Revealed by Atomic Resolution Analyses of Endoglucanase Cel5A
Acta Crystallogr.,Sect.D, 59:447-, 2003

PubMed Abstract: Non-covalent interactions between protein and ligand at the active centre of glycosidases play an enormous role in catalysis. Dissection of these hydrogen-bonding networks is not merely important for an understanding of enzymatic catalysis, but is also increasingly relevant for the design of transition-state mimics, whose tautomeric state, hydrogen-bonding interactions and protonation contribute to tight binding. Here, atomic resolution ( approximately 1 A) analysis of a series of complexes of the 34 kDa catalytic core domain of the Bacillus agaradhaerens endoglucanase Cel5A is presented. Cel5A is a 'retaining' endoglucanase which performs catalysis via the formation and subsequent breakdown of a covalent glycosyl-enzyme intermediate via oxocarbenium-ion-like transition states. Previous medium-resolution analyses of a series of enzymatic snapshots has revealed conformational changes in the substrate along the reaction coordinate (Davies et al., 1998). Here, atomic resolution analyses of the series of complexes along the pathway are presented, including the 'Michaelis' complex of the unhydrolysed substrate, the covalent glycosyl-enzyme intermediate and the complex with the reaction product, cellotriose. These structures reveal intimate details of the protein-ligand interactions, including most of the carbohydrate-associated H atoms and the tautomeric state of crucial active-centre groups in the pH 5 orthorhombic crystal form and serve to illustrate the potential for atomic resolution analyses to inform strategies for enzyme inhibition.

PubMed: 12595701
DOI: 10.1107/S0907444902023405

実験手法

X-RAY DIFFRACTION (1.15 Å)