# 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}
}
• Published 13 May 1967
• Chemistry
• Nature
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…
489 Citations
Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?
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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.
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• 1972
2.8-A structure of yeast serine carboxypeptidase.
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• 1994
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.
Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products.
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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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