title: Conformational change in substrate binding, catalysis and product release: an open and shut case?
abstract: The role of conformational change in substrate binding, catalysis and product release is reviewed for 11 enzymes, for which crystal structures are available for the apo, substrate- and product-bound states. The extent of global conformational changes is measured, and the movements of the functional regions involved in catalysis and ligand binding are compared to the rest of the structure. We find that most of these enzymes undergo relatively small amounts of conformational change and particularly small changes in catalytic residue geometry, usually less than 1 A. In some enzymes there is significant movement of the binding residues, usually on surface loops.
authors.affiliation: EBI, Wellcome Trust Genome Campus, Hinxton, Cambridgeshire CB10 1SD, UK. alexg@ebi.ac.uk
authors.forename: Alex
authors.initials: A
authors.lastname: Gutteridge
authors.forename: Janet
authors.initials: J
authors.lastname: Thornton
mesh_terms: D002384:Catalysis; D018360:Crystallography, X-Ray; D019992:Databases as Topic; D004798:Enzymes / Q000737:chemistry*; D008024:Ligands; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D013379:Substrate Specificity
chemical_list: D004798:Enzymes; D008024:Ligands; D011506:Proteins