1IA7

CRYSTAL STRUCTURE OF THE CELLULASE CEL9M OF C. CELLULOLYTICIUM IN COMPLEX WITH CELLOBIOSE

1IA7 の概要

• エントリーDOI: 10.2210/pdb1ia7/pdb
• 関連するPDBエントリー: 1CLC 1IA7 1JS4
• 関連するBIRD辞書のPRD_ID: PRD_900005
• 分子名称: CELLULASE CEL9M, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, CALCIUM ION, ... (8 entities in total)
• 機能のキーワード: cellulase, alpha barrel, hydrolase
• 由来する生物種: Clostridium cellulolyticum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49486.62

構造登録者

Parsiegla, G.,Belaich, A.,Belaich, J.P.,Haser, R. (登録日: 2001-03-22, 公開日: 2002-10-30, 最終更新日: 2023-08-09)

主引用文献

Parsiegla, G.,Belaich, A.,Belaich, J.P.,Haser, R.
Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases.
Biochemistry, 41:11134-11142, 2002

PubMed Abstract: Cellulases cleave the beta-1.4 glycosidic bond of cellulose. They have been characterized as endo or exo and processive or nonprocessive cellulases according to their action mode on the substrate. Different types of these cellulases may coexist in the same glycoside hydrolase family, which have been classified according to their sequence homology and catalytic mechanism. The bacterium C. celluloyticum produces a set of different cellulases who belong mostly to glycoside hydrolase families 5 and 9. As an adaptation of the organism to different macroscopic substrates organizations and to maximize its cooperative digestion, it is expected that cellulases of these families are active on the various macroscopic organizations of cellulose chains. The nonprocessive cellulase Cel9M is the shortest variant of family 9 cellulases (subgroup 9(C)) which contains only the catalytic module to interact with the substrate. The crystal structures of free native Cel9M and its complex with cellobiose have been solved to 1.8 and 2.0 A resolution, respectively. Other structurally known family 9 cellulases are the nonprocessive endo-cellulase Cel9D from C. thermocellum and the processive endo-cellulase Cel9A from T. fusca, from subgroups 9(B1) and 9(A), respectively, whose catalytic modules are fused to a second domain. These enzymes differ in their activity on substrates with specific macroscopic appearances. The comparison of the catalytic module of Cel9M with the two other known GH family 9 structures may give clues to explain its substrate profile and action mode.

PubMed: 12220178
DOI: 10.1021/bi025816m

実験手法

X-RAY DIFFRACTION (2 Å)