PDBsum entry 1ga2

Hydrolase

PDB id: 1ga2

Contents

Protein chains

611 a.a. *

Ligands

BGC-BGC-BGC

BGC-BGC ×2

GOL ×5

ACY

Metals

_CA ×4

_MG ×7

Waters ×757

* Residue conservation analysis

References listed in PDB file

Key reference

• Title: X-Ray crystal structure of the multidomain endoglucanase cel9g from clostridium cellulolyticum complexed with natural and synthetic cello-Oligosaccharides.
• Authors: D.Mandelman, A.Belaich, J.P.Belaich, N.Aghajari, H.Driguez, R.Haser.
• Ref.: J Bacteriol, 2003, 185, 4127-4135.
• PubMed id: 12837787

Abstract

Complete cellulose degradation is the first step in the use of biomass as a source of renewable energy. To this end, the engineering of novel cellulase activity, the activity responsible for the hydrolysis of the beta-1,4-glycosidic bonds in cellulose, is a topic of great interest. The high-resolution X-ray crystal structure of a multidomain endoglucanase from Clostridium cellulolyticum has been determined at a 1.6-A resolution. The endoglucanase, Cel9G, is comprised of a family 9 catalytic domain attached to a family III(c) cellulose-binding domain. The two domains together form a flat platform onto which crystalline cellulose is suggested to bind and be fed into the active-site cleft for endolytic hydrolysis. To further dissect the structural basis of cellulose binding and hydrolysis, the structures of Cel9G in the presence of cellobiose, cellotriose, and a DP-10 thio-oligosaccharide inhibitor were resolved at resolutions of 1.7, 1.8, and 1.9 A, respectively.