Structure of acid protease from Endothia parasitica in crosslinked form at 2.45-.ANG. resolution
- 17 April 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (8) , 1638-1640
- https://doi.org/10.1021/bi00575a041
Abstract
The structure of acid protease from E. parasitica in strongly cross-linked form is compared with that of the untreated protein at 2.45 .ANG. resolution. The only observed conformation change introduced by the cross-linking reaction is at the N terminal. The 2 main chain structures are essentially identical. Approximately 2 molecules of the inhibitor, 1,2-epoxy-3-(p-nitrophenoxy)propane, are incorporated into each protein molecule. They are covalently bound to the 2 aspartic residues at the active center.This publication has 4 references indexed in Scilit:
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- Intermolecular cross-linking of a protein crystal - acid protease from endothia parasitica - in 2.7 M ammonium sulfate solutionBiochemical and Biophysical Research Communications, 1978
- Mechanism of acid protease catalysis based on the crystal structure of penicillopepsinNature, 1977
- The Enzymic Behavior of Carboxypeptidase-A in the Solid State*Biochemistry, 1966