Analysis of an enzyme-substrate complex by x-ray crystallography and transferred nuclear overhauser enhancement measurements: porcine pancreatic elastase and a hexapeptide
- 26 January 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 27 (2) , 725-730
- https://doi.org/10.1021/bi00402a035
Abstract
The hexapeptide substrate Thr-Pro-n Val-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-.ANG. resolution were used in the structure analysis with refinement to an R-factor of 0.19.This publication has 12 references indexed in Scilit:
- Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin.The EMBO Journal, 1986
- Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distancesJournal of Molecular Biology, 1984
- Stereochemistry of ATP and GTP bound to fish haemoglobinsJournal of Molecular Biology, 1984
- An unusual conformation of NAD+ bound to sorbitoldehydrogenase?Journal of Molecular Biology, 1984
- Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-.ANG. resolutionBiochemistry, 1983
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1983
- Proton nuclear magnetic resonance studies on cyclic nucleotide binding to the Escherichia coli adenosine cyclic 3',5'-phosphate receptor proteinBiochemistry, 1982
- Conformation of NAD+ bound to yeast and horse liver alcohol dehydrogenase in solutionJournal of Molecular Biology, 1982
- Stereochemical aspects of peptide hydrolysis catalyzed by serine proteases of the chymotrypsin typeBioorganic Chemistry, 1981