V. Kh. Akparov, G. E. Konstantinova, V. I. Timofeev, M. B. Shevtsov, I. P. Kuranova
{"title":"Structure of Carboxypeptidase T from Thermoactinomyces Vulgaris in Complex with L-Phenyl Lactate","authors":"V. Kh. Akparov, G. E. Konstantinova, V. I. Timofeev, M. B. Shevtsov, I. P. Kuranova","doi":"10.1134/s1063774524600315","DOIUrl":null,"url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>The crystal structure of metallocarboxypeptidase T (CPT) from <i>Thermoactinomyces vulgaris</i> in complex with <i>L</i>-phenyl lactate was determined at 1.73 Å resolution. As opposed to pancreatic carboxypeptidase A, which binds one <i>L</i>-phenyl lactate molecule, the ligand in the complex with CPT occupies simultaneously the S1 and S' subsites of the active site. This leads to conformational changes, which differ from those caused by the alternating occupation of the S1 and S1' subsites by <i>tert</i>-butyloxycarbonyl-<i>L</i>-leucine (BOC-leucine) and benzylsuccinic acid. These changes concern the residues E277, E59, L254, G192, S127, and Y218 and are up to 0.77 Å. A conclusion was drawn about the possible role of the residue E59 in the substrate recognition and catalysis by carboxypeptidase Т.</p>","PeriodicalId":527,"journal":{"name":"Crystallography Reports","volume":null,"pages":null},"PeriodicalIF":0.6000,"publicationDate":"2024-07-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Crystallography Reports","FirstCategoryId":"88","ListUrlMain":"https://doi.org/10.1134/s1063774524600315","RegionNum":4,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CRYSTALLOGRAPHY","Score":null,"Total":0}
引用次数: 0
Abstract
The crystal structure of metallocarboxypeptidase T (CPT) from Thermoactinomyces vulgaris in complex with L-phenyl lactate was determined at 1.73 Å resolution. As opposed to pancreatic carboxypeptidase A, which binds one L-phenyl lactate molecule, the ligand in the complex with CPT occupies simultaneously the S1 and S' subsites of the active site. This leads to conformational changes, which differ from those caused by the alternating occupation of the S1 and S1' subsites by tert-butyloxycarbonyl-L-leucine (BOC-leucine) and benzylsuccinic acid. These changes concern the residues E277, E59, L254, G192, S127, and Y218 and are up to 0.77 Å. A conclusion was drawn about the possible role of the residue E59 in the substrate recognition and catalysis by carboxypeptidase Т.
期刊介绍：
Crystallography Reports is a journal that publishes original articles short communications, and reviews on various aspects of crystallography: diffraction and scattering of X-rays, electrons, and neutrons, determination of crystal structure of inorganic and organic substances, including proteins and other biological substances; UV-VIS and IR spectroscopy; growth, imperfect structure and physical properties of crystals; thin films, liquid crystals, nanomaterials, partially disordered systems, and the methods of studies.
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