Three-dimensional structure of recombinant carboxypeptidase T from Thermoactinomyces vulgaris without calcium ions View Full Text


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Article Info

DATE

2011-07

AUTHORS

V. Kh. Akparov, V. I. Timofeev, I. P. Kuranova

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-Å 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. More... »

PAGES

596

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s106377451104002x

DOI

http://dx.doi.org/10.1134/s106377451104002x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1047792718


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