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Title: Three-dimensional structure of recombinant carboxypeptidase T from Thermoactinomyces vulgaris without calcium ions

Abstract

Crystals of recombinant carboxypeptidase T (CPT) from Thermoactinomyces vulgaris were grown in a capillary by the counterdiffusion method in the absence of calcium ions. The three-dimensional structure of CPT was solved at 1.69- Angstrom-Sign resolution using the X-ray diffraction data collected from the crystals of the enzyme on the SPring-8 synchrotron radiation facility and was then refined to Rfact = 16.903% and Rfree = 18.165%. The coordinates of the refined model were deposited in the Protein Data Bank (PDB ID: 3QNV). A comparison of this structure with the structure of wild-type CPT containing bound calcium ions, which was determined earlier, revealed a number of conformational changes both in the calcium-binding sites and the enzyme active site. Based on the results of this comparison, the possible factors responsible for the difference in the catalytic activity of the two forms of the enzyme are considered.

Authors:
 [1]; ;  [2]
  1. Scientific Center of Russian Federation Research Institute for Genetics and Selection of Industrial Microorganisms (Russian Federation)
  2. Russian Academy of Sciences, Shubnikov Institute of Crystallography (Russian Federation)
Publication Date:
OSTI Identifier:
22054275
Resource Type:
Journal Article
Journal Name:
Crystallography Reports
Additional Journal Information:
Journal Volume: 56; Journal Issue: 4; Other Information: Copyright (c) 2011 Pleiades Publishing, Ltd.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1063-7745
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CALCIUM IONS; CARBOXYPEPTIDASES; COMPARATIVE EVALUATIONS; CONFORMATIONAL CHANGES; CRYSTALS; MOLECULAR STRUCTURE; SPRING-8 STORAGE RING; SYNCHROTRON RADIATION; THERMOACTINOMYCES; X-RAY DIFFRACTION

Citation Formats

Akparov, V. Kh., E-mail: valery@akparov.ru, Timofeev, V. I., E-mail: inna@ns.crys.ras.ru, and Kuranova, I. P. Three-dimensional structure of recombinant carboxypeptidase T from Thermoactinomyces vulgaris without calcium ions. United States: N. p., 2011. Web. doi:10.1134/S106377451104002X.
Akparov, V. Kh., E-mail: valery@akparov.ru, Timofeev, V. I., E-mail: inna@ns.crys.ras.ru, & Kuranova, I. P. Three-dimensional structure of recombinant carboxypeptidase T from Thermoactinomyces vulgaris without calcium ions. United States. doi:10.1134/S106377451104002X.
Akparov, V. Kh., E-mail: valery@akparov.ru, Timofeev, V. I., E-mail: inna@ns.crys.ras.ru, and Kuranova, I. P. Fri . "Three-dimensional structure of recombinant carboxypeptidase T from Thermoactinomyces vulgaris without calcium ions". United States. doi:10.1134/S106377451104002X.
@article{osti_22054275,
title = {Three-dimensional structure of recombinant carboxypeptidase T from Thermoactinomyces vulgaris without calcium ions},
author = {Akparov, V. Kh., E-mail: valery@akparov.ru and Timofeev, V. I., E-mail: inna@ns.crys.ras.ru and Kuranova, I. P.},
abstractNote = {Crystals of recombinant carboxypeptidase T (CPT) from Thermoactinomyces vulgaris were grown in a capillary by the counterdiffusion method in the absence of calcium ions. The three-dimensional structure of CPT was solved at 1.69- Angstrom-Sign resolution using the X-ray diffraction data collected from the crystals of the enzyme on the SPring-8 synchrotron radiation facility and was then refined to Rfact = 16.903% and Rfree = 18.165%. The coordinates of the refined model were deposited in the Protein Data Bank (PDB ID: 3QNV). A comparison of this structure with the structure of wild-type CPT containing bound calcium ions, which was determined earlier, revealed a number of conformational changes both in the calcium-binding sites and the enzyme active site. Based on the results of this comparison, the possible factors responsible for the difference in the catalytic activity of the two forms of the enzyme are considered.},
doi = {10.1134/S106377451104002X},
journal = {Crystallography Reports},
issn = {1063-7745},
number = 4,
volume = 56,
place = {United States},
year = {2011},
month = {7}
}