Structural highlights
Function
[CBPT_THEVU] Able to split off hydrophobic and basic amino acids with comparable efficiency.
Publication Abstract from PubMed
The 3D structure of recombinant bacterial carboxypeptidase T (CPT) in complex with N-BOC-L-leucine was determined at 1.38 A 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.
Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine.,Timofeev VI, Kuznetsov SA, Akparov VKh, Chestukhina GG, Kuranova IP Biochemistry (Mosc). 2013 Mar;78(3):252-9. doi: 10.1134/S0006297913030061. PMID:23586718[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Timofeev VI, Kuznetsov SA, Akparov VKh, Chestukhina GG, Kuranova IP. Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine. Biochemistry (Mosc). 2013 Mar;78(3):252-9. doi: 10.1134/S0006297913030061. PMID:23586718 doi:http://dx.doi.org/10.1134/S0006297913030061
