X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides.
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.
Mandelman
David
D
Laboratoire de BioCristallographie, Institut de Biologie et Chimie des Protéines, UMR 5086, CNRS et Université Claude Bernard Lyon I, 69367 Lyon, Cedex 07, France.
Belaich
Anne
A
Belaich
J P
JP
Aghajari
Nushin
N
Driguez
Hugues
H
Haser
Richard
R
D000595:Amino Acid Sequence; D001665:Binding Sites; D002475:Cellobiose / Q000378:metabolism; D002480:Cellulase / Q000737:chemistry* / Q000378:metabolism; D002482:Cellulose / Q000378:metabolism*; D003013:Clostridium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000378:metabolism*; D011487:Protein Conformation; D016415:Sequence Alignment
D009844:Oligosaccharides; D002475:Cellobiose; D002482:Cellulose; D002480:Cellulase