1KFG

The X-ray Crystal Structure of Cel9G from Clostridium cellulolyticum complexed with a Thio-Oligosaccharide Inhibitor

Summary for 1KFG

• Entry DOI: 10.2210/pdb1kfg/pdb
• Related: 1G87 1GA7 1K72
• Descriptor: ENDOGLUCANASE G, 4-thio-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-4-thio-beta-D-glucopyranose-(1-4)-1-thio-beta-D-glucopyranose, CALCIUM ION, ... (8 entities in total)
• Functional Keywords: endoglucanase, family 9, thio-oligosaccharide, cellulose binding domain, (alpha-alpha)6-barrel, hydrolase
• Biological source: Clostridium cellulolyticum
• Total number of polymer chains: 2
• Total formula weight: 138382.77

Authors

Mandelman, D.,Belaich, A.,Belaich, J.-P.,Driguez, H.,Haser, R. (deposition date: 2001-11-20, release date: 2003-07-15, Last modification date: 2023-08-16)

Primary citation

Mandelman, D.,Belaich, A.,Belaich, J.-P.,Aghajari, N.,Driguez, H.,Haser, R.
The X-ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-olligosaccharides
J.Bacteriol., 185:4127-4135, 2003

PubMed 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.

PubMed: 12837787
DOI: 10.1128/JB.185.14.4127-4135.2003

Experimental method

X-RAY DIFFRACTION (1.9 Å)