1ga2
From Proteopedia
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THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM COMPLEXED WITH CELLOBIOSE
Overview
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.
About this Structure
1GA2 is a Single protein structure of sequence from Clostridium cellulolyticum with CA, MG, GOL and ACY as ligands. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.
Reference
X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides., Mandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R, J Bacteriol. 2003 Jul;185(14):4127-35. PMID:12837787
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