Structure of the microbial carboxypeptidase T complexed with the transition state analog N-sulfamoyl-l-lysine.
Autor: | Akparov VK; National Research Center 'Kurchatov institute', Ak. Kurchatova square 1, Moscow 123182, Russian Federation. Electronic address: valery.akparov@yandex.ru., Konstantinova GE; National Research Center 'Kurchatov institute', Ak. Kurchatova square 1, Moscow 123182, Russian Federation., Timofeev VI; Shubnikov Institute of Crystallography of Federal Scientific Research Centre 'Crystallography and Photonics' Russian Academy of Sciences, Leninskii Prospect 59, Moscow 119333, Russian Federation., Khaliullin IG; Moscow Institute of Physics and Technology (State University), 9 Institutsky per. Dolgoprudny, Moscow Region 141700, Russian Federation., Kuranova IP; Shubnikov Institute of Crystallography of Federal Scientific Research Centre 'Crystallography and Photonics' Russian Academy of Sciences, Leninskii Prospect 59, Moscow 119333, Russian Federation. |
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Jazyk: | angličtina |
Zdroj: | Biophysical chemistry [Biophys Chem] 2021 Mar; Vol. 270, pp. 106535. Date of Electronic Publication: 2020 Dec 23. |
DOI: | 10.1016/j.bpc.2020.106535 |
Abstrakt: | Carboxypeptidase T (CPT) from Thermoactinomyces vulgaris (EC 3.4.17.18) has a broad substrate specificity, the mechanism of which remains unclear. It cleaves off arginine residues by 10, and lysine residues by 100 times worse than hydrophobic leucine residues despite the presence of negatively charged Asp260 at the bottom of the primary specificity pocket. To study the relationship between the structure and specificity the 3D structure of CPT in complex with the stable transition state analog N-sulfamoyl-l-lysine (SLys) was determined in which the S-atom imitates the sp3-hybridized carbon in the scissile-bond. Crystals grown in microgravity has the symmetry of space group P6 (Copyright © 2020. Published by Elsevier B.V.) |
Databáze: | MEDLINE |
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