Three-dimensional Structure of Tosyl-α-chymotrypsin

@article{Matthews1967ThreedimensionalSO,
  title={Three-dimensional Structure of Tosyl-$\alpha$-chymotrypsin},
  author={Brian W. Matthews and Paul B. Sigler and Richard Henderson and David M. Blow},
  journal={Nature},
  year={1967},
  volume={214},
  pages={652-656}
}
A model is proposed for the structure of an inhibited derivative of an enzyme which hydrolyses proteins. It is based on a map of the electron density distribution at 2 Å resolution and interpreted in terms of a previously reported sequence of 241 amino-acids. The map has been derived from a Fourier synthesis of 24,500 terms and represents two crystallographically independent molecules, each of molecular weight 25,000, which are nearly identical in their tertiary structure. The enzyme is… 
Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?
TLDR
The crystallographic refinement provides a detailed geometrical description of the enzyme-substrate-solvent interactions that occur in the presumptive adduct and suggests that gamma-chymotrypsin may not be the free enzyme but rather a complex, possibly an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr.
Structure of crystalline methyl-chymotrypsin.
2.8-A structure of yeast serine carboxypeptidase.
TLDR
A surprising result of the study is that the domains consisting of residues 180-317, which form a largely alpha-helical insertion into the highly conserved cores surrounding the active site, are quite different structurally in the two molecules.
6 The Structure of Chymotrypsin
Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products.
TLDR
HPLC analyses of the enzyme before and after crystallization demonstrated the presence of a wide variety of oligopeptides in the redissolved crystal, most with COOH-terminal aromatic residues, as expected of the products of chymotrypsin cleavage.
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