Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris

A. Teplyakov, K. Polyakov, G. Obmolova, B. Strokopytov, I. Kuranova, A. Osterman, N. Grishin, S. Smulevitch, O. Zagnitko, O. Galperina, M. Matz, V. Stepanov

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20 Scopus citations


The crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris has been determined at 0.235‐nm resolution by X‐ray diffraction. Carboxypeptidase T is a remote homologue of mammalian Zn‐carboxypeptidases. In spite of the low degree of amino acid sequence identity, the three‐dimensional structure of carboxypeptidase T is very similar to that of pancreatic carboxypeptidases A and B. The core of the protein molecule is formed by an eight‐stranded mixed β sheet. The active site is located at the C‐edge of the central (parallel) part of the β sheet. The structural organization of the active centre appears to be essentially the same in the three carboxypeptidases. Amino acid residues directly involved in catalysis and binding of the C‐terminal carboxyl of a substrate are strictly conserved. This suggests that the catalytic mechanism proposed for the pancreatic enzymes is applicable to carboxypeptidase T and to the whole family of Zn‐carboxypeptidases. Comparison of the amino acid replacements at the primary specificity pocket of carboxypeptidases A, B and T provides an explanation of the unusual ‘A + B’ type of specificity of carboxypeptidase T. Four calcium‐binding sites localized in the crystal structure of carboxypeptidase T could account for the high thermostability of the protein.

Original languageEnglish (US)
Pages (from-to)281-288
Number of pages8
JournalEuropean Journal of Biochemistry
Issue number2
StatePublished - Sep 1992

ASJC Scopus subject areas

  • Biochemistry


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