4F8Z

Carboxypeptidase T with Boc-Leu

Summary for 4F8Z

• Entry DOI: 10.2210/pdb4f8z/pdb
• Descriptor: Carboxypeptidase T, ZINC ION, N-(tert-butoxycarbonyl)-L-leucine, ... (7 entities in total)
• Functional Keywords: hydrolase
• Biological source: Thermoactinomyces vulgaris
• Total number of polymer chains: 1
• Total formula weight: 39412.54

Authors

Timofeev, V.I.,Kuznetsov, S.A.,Akparov, V.K.,Kuranova, I.P. (deposition date: 2012-05-18, release date: 2013-05-22, Last modification date: 2024-11-27)

Primary citation

Timofeev, V.I.,Kuznetsov, S.A.,Akparov, V.K.h.,Chestukhina, G.G.,Kuranova, I.P.
Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine.
Biochemistry Mosc., 78:252-259, 2013

PubMed 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.

PubMed: 23586718
DOI: 10.1134/S0006297913030061

Experimental method

X-RAY DIFFRACTION (1.38 Å)