Motion in Family-5 Endoglucanase CelC [eg]

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Classification Known Domain Motion, Hinge Mechanism [D-h-2]

Structures 1CEC Conformation 1 [ PartsList ] 1CEN Mutant, with ligand [ PartsList ] 1CEO Mutant [ PartsList ]

Description Comparison of the unliganded and liganded crystallographic structures (not yet available from PDB as of October 1997) revealed conformational changes resulting from substrate binding, including a significant reorientation of the loop 138-141, which carries the general acid/base catalyst Glu140 in the wild-type endoglucanase CelC. Upon substrate binding, significant conformational changes are observed in residues 139-141 and 95-103. Residue 140 in the complex structure is shifted by approximately 3 A with respect to the unliganded structure, and has its side change rotated about 90 degrees. The carbonyl oxygen atoms of residues 139 and 140 are brought into close proximity upon substrate binding, resulting in an induced fit movement of loops 95-103 and 138-141.

Particular values describing motion Maximum CA displacement (A) = 3 ((from article)) Experimental Methods = x (Traditional x-ray) Creation Date = 19971130 Modification Date = 19971130

References Dominguez R, Souchon H, Lascombe M, Alzari PM (1996). The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism. J Mol Biol 257(5):1042-1051. [Medline info for 96192088]

GO terms associated with structures Molecular function hydrolase activity, hydrolyzing O-glycosyl compounds Biological process carbohydrate metabolism

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu