title: Protein structural change upon ligand binding correlates with enzymatic reaction mechanism.
abstract: Overall structural changes of enzymes in response to ligand binding were investigated by database analysis of 62 non-redundant enzymes whose ligand-unbound and ligand-bound forms were available in the Protein Data Bank. The results of analysis indicate that transferases often undergo large rigid-body domain motions upon ligand binding, while other enzymes, most typically, hydrolases, change their structures to a small extent. It was also found that the solvent accessibility of the substrate molecule was low in transferases but high in hydrolases. These differences are explained by the enzymatic reaction mechanisms. The transferase reaction requires the catalytic groups to be insulated from the water environment, and thus transferases bury the ligand molecule inside the protein by closing the cleft. On the other hand, the hydrolase reaction involves the surrounding water molecules and occurs at the protein surface, requiring only a small structural change.
authors.affiliation: Global Scientific Information and Computing Center, Tokyo Institute of Technology, O-okayama, Tokyo 152-8550, Japan.
authors.forename: Ryotaro
authors.initials: R
authors.lastname: Koike
authors.forename: Takayuki
authors.initials: T
authors.lastname: Amemiya
authors.forename: Motonori
authors.initials: M
authors.lastname: Ota
authors.forename: Akinori
authors.initials: A
authors.lastname: Kidera
mesh_terms: D001665:Binding Sites; D030562:Databases, Protein; D004798:Enzymes / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D012997:Solvents / Q000737:chemistry
chemical_list: D004798:Enzymes; D008024:Ligands; D012997:Solvents