Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2013-03

AUTHORS

V. I. Timofeev, S. A. Kuznetsov, V. Kh. Akparov, G. G. Chestukhina, I. P. Kuranova

ABSTRACT

The 3D structure of recombinant bacterial carboxypeptidase T (CPT) in complex with N-BOC-L-leucine was determined at 1.38 Å resolution. Crystals for the X-ray study were grown in microgravity using the counter-diffusion technique. N-BOC-L-leucine and SO4(2-) ion bound in the enzyme active site were localized in the electron density map. Location of the leucine side chain in CPT-N-BOC-L-leucine complex allowed identification of the S1 subsite of the enzyme, and its structure was determined. Superposition of the structures of CPT-N-BOC-L-leucine complex and complexes of pancreatic carboxypeptidases A and B with substrate and inhibitors was carried out, and similarity of the S1 subsites in these three carboxypeptidases was revealed. It was found that SO4(2-) ion occupies the same position in the S1' subsite as the C-terminal carboxy group of the substrate. More... »

PAGES

252-259

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s0006297913030061

DOI

http://dx.doi.org/10.1134/s0006297913030061

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005218667

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23586718


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