1obr
From Proteopedia
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CARBOXYPEPTIDASE T
Overview
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 beta sheet. The, active site is located at the C-edge of the central (parallel) part of the, beta 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.
About this Structure
1OBR is a Single protein structure of sequence from Thermoactinomyces vulgaris with ZN, CA and SO4 as ligands. Active as Carboxypeptidase T, with EC number 3.4.17.18 Full crystallographic information is available from OCA.
Reference
Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris., Teplyakov A, Polyakov K, Obmolova G, Strokopytov B, Kuranova I, Osterman A, Grishin N, Smulevitch S, Zagnitko O, Galperina O, et al., Eur J Biochem. 1992 Sep 1;208(2):281-8. PMID:1521526
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