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Structure of the carboxypeptidase t from <i>Thermoactinomyces vulgaris</i> complex with <i>L</i> - phenyl lactate
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Structure of the carboxypeptidase t from <i>Thermoactinomyces vulgaris</i> complex with <i>L</i> - phenyl lactate
Annotation
PII
S0023476124030067-1
Publication type
Article
Status
Published
Authors
V. Kh. Akparov 
Affiliation:
Shubnikov Institute of Crystallography of Kurchatov Complex of Crystallography and Photonics of NRC “Kurchatov Institute”
Moscow Institute of Physics and Technology
Edition
Volume 69 Issue number 3
Pages
422-428
Abstract
The crystal structure of the metallocarboxypeptidase T from Thermoactinomyces vulgaris complex with L-phenylactate was obtained with a resolution of 1.73 Å. Unlike pancreatic carboxypeptidase A, which binds one L-phenylactate molecule, in complex with CPT, the ligand occupies both S1 and S1ʹ sites of the active center simultaneously. In this case, conformational changes occur that differ from the changes caused by the alternate occupation of the S1 and S1ʹ sites by BOC-leucine and benzylsuccinic acid. These changes concern the residues E277, E59, L254, G192, S127 and Y218 and reach a span of 0.77 Å. A conclusion is made about the possible role of these residues in the recognition and catalysis of substrates by carboxypeptidase T.
Acknowledgment
Government of the Russian Federation, state assignment.
Received
04.09.2024
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