title: Analysis of an enzyme-substrate complex by X-ray crystallography and transferred nuclear Overhauser enhancement measurements: porcine pancreatic elastase and a hexapeptide.
abstract: The hexapeptide substrate Thr-Pro-nVal-NMeLeu-Tyr-Thr reacts with porcine pancreatic elastase sufficiently slowly that accelerated crystallographic data collection procedures and two-dimensional transferred nuclear Overhauser enhancement measurements could be used to study the geometry of binding. Both studies report a time-averaged population of the Michaelis complex state, prior to proteolysis. This result provides an important data point along the reaction coordinate pathway for serine proteases. Crystallographic data to 1.80-A resolution were used in the structure analysis with refinement to an R-factor of 0.19.
authors.affiliation: Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843-2128.
authors.forename: E F
authors.initials: EF
authors.lastname: Meyer
authors.forename: G M
authors.initials: GM
authors.lastname: Clore
authors.forename: A M
authors.initials: AM
authors.lastname: Gronenborn
authors.forename: H A
authors.initials: HA
authors.lastname: Hansen
mesh_terms: D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D009842:Oligopeptides / Q000378:metabolism*; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013552:Swine; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D009842:Oligopeptides; D010196:Pancreatic Elastase