4 results on '"Daniil D. Vakhrameev"'
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2. XANES Measurements for Studies of Adsorbed Protein Layers at Liquid Interfaces
- Author
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Oleg V. Konovalov, Natalia N. Novikova, Mikhail V. Kovalchuk, Galina E. Yalovega, Alexey F. Topunov, Olga V. Kosmachevskaya, Eleonora A. Yurieva, Alexander V. Rogachev, Alexander L. Trigub, Maria A. Kremennaya, Valentin I. Borshchevskiy, Daniil D. Vakhrameev, and Sergey N. Yakunin
- Subjects
metalloproteins ,XANES ,zinc binding sites ,protein layers at liquid interface ,Langmuir trough ,Technology ,Electrical engineering. Electronics. Nuclear engineering ,TK1-9971 ,Engineering (General). Civil engineering (General) ,TA1-2040 ,Microscopy ,QH201-278.5 ,Descriptive and experimental mechanics ,QC120-168.85 - Abstract
X-ray absorption near edge structure (XANES) spectra for protein layers adsorbed at liquid interfaces in a Langmuir trough have been recorded for the first time. We studied the parkin protein (so-called E3 ubiquitin ligase), which plays an important role in pathogenesis of Parkinson disease. Parkin contains eight Zn binding sites, consisting of cysteine and histidine residues in a tetracoordinated geometry. Zn K-edge XANES spectra were collected in the following two series: under mild radiation condition of measurements (short exposition time) and with high X-ray radiation load. XANES fingerprint analysis was applied to obtain information on ligand environments around zinc ions. Two types of zinc coordination geometry were identified depending on X-ray radiation load. We found that, under mild conditions, local zinc environment in our parkin preparations was very similar to that identified in hemoglobin, treated with a solution of ZnCl2 salt. Under high X-ray radiation load, considerable changes in the zinc site structure were observed; local zinc environment appeared to be almost identical to that defined in Zn-containing enzyme alkaline phosphatase. The formation of a similar metal site in unrelated protein molecules, observed in our experiments, highlights the significance of metal binding templates as essential structural modules in protein macromolecules.
- Published
- 2020
- Full Text
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3. Structural basis for receptor selectivity and inverse agonism in S1P 5 receptors.
- Author
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Lyapina E, Marin E, Gusach A, Orekhov P, Gerasimov A, Luginina A, Vakhrameev D, Ergasheva M, Kovaleva M, Khusainov G, Khorn P, Shevtsov M, Kovalev K, Bukhdruker S, Okhrimenko I, Popov P, Hu H, Weierstall U, Liu W, Cho Y, Gushchin I, Rogachev A, Bourenkov G, Park S, Park G, Hyun HJ, Park J, Gordeliy V, Borshchevskiy V, Mishin A, and Cherezov V
- Subjects
- Humans, Immune System, Lysophospholipids pharmacology, Receptors, Lysosphingolipid, Sphingosine analogs & derivatives, Sphingosine pharmacology
- Abstract
The bioactive lysophospholipid sphingosine-1-phosphate (S1P) acts via five different subtypes of S1P receptors (S1PRs) - S1P
1-5 . S1P5 is predominantly expressed in nervous and immune systems, regulating the egress of natural killer cells from lymph nodes and playing a role in immune and neurodegenerative disorders, as well as carcinogenesis. Several S1PR therapeutic drugs have been developed to treat these diseases; however, they lack receptor subtype selectivity, which leads to side effects. In this article, we describe a 2.2 Å resolution room temperature crystal structure of the human S1P5 receptor in complex with a selective inverse agonist determined by serial femtosecond crystallography (SFX) at the Pohang Accelerator Laboratory X-Ray Free Electron Laser (PAL-XFEL) and analyze its structure-activity relationship data. The structure demonstrates a unique ligand-binding mode, involving an allosteric sub-pocket, which clarifies the receptor subtype selectivity and provides a template for structure-based drug design. Together with previously published S1PR structures in complex with antagonists and agonists, our structure with S1P5 -inverse agonist sheds light on the activation mechanism and reveals structural determinants of the inverse agonism in the S1PR family., (© 2022. The Author(s).)- Published
- 2022
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4. A new twist of rubredoxin function in M. tuberculosis.
- Author
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Sushko T, Kavaleuski A, Grabovec I, Kavaleuskaya A, Vakhrameev D, Bukhdruker S, Marin E, Kuzikov A, Masamrekh R, Shumyantseva V, Tsumoto K, Borshchevskiy V, Gilep A, and Strushkevich N
- Subjects
- Calorimetry, Circular Dichroism, Cloning, Molecular, Crystallization, Cytochrome P-450 Enzyme System chemistry, Cytochrome P-450 Enzyme System metabolism, Electron Transport, Gene Expression Regulation, Bacterial, Models, Molecular, Mutagenesis, Site-Directed, Oxidation-Reduction, Protein Binding, Protein Conformation, Rubredoxins chemistry, Zinc chemistry, Zinc metabolism, Mycobacterium tuberculosis metabolism, Rubredoxins metabolism
- Abstract
Electron transfer mediated by metalloproteins drives many biological processes. Rubredoxins are a ubiquitous [1Fe-0S] class of electron carriers that play an important role in bacterial adaptation to changing environmental conditions. In Mycobacterium tuberculosis, oxidative and acidic stresses as well as iron starvation induce rubredoxins expression. However, their functions during M. tuberculosis infection are unknown. In the present work, we show that rubredoxin B (RubB) is able to efficiently shuttle electrons from cognate reductases, FprA and FdR to support catalytic activity of cytochrome P450s, CYP124, CYP125, and CYP142, which are important for bacterial viability and pathogenicity. We solved the crystal structure of RubB and characterized the interaction between RubB and CYPs using site-directed mutagenesis. Mutations that not only neutralize single charge but also change the specific residues on the surface of RubB did not dramatically decrease activity of studied CYPs. Together with isothermal calorimetry (ITC) experiments, the obtained results suggest that interactions are transient and not highly specific. The redox potential of RubB is -264 mV vs. Ag/AgCl and the measured extinction coefficients are 9931 M
-1 cm-1 and 8371 M-1 cm-1 at 380 nm and 490 nm, respectively. Characteristic parameters of RubB along with the discovered function might be useful for biotechnological applications. Our findings suggest that a switch from ferredoxins to rubredoxins might be crucial for M. tuberculosis to support CYPs activity during the infection., (Copyright © 2021 Elsevier Inc. All rights reserved.)- Published
- 2021
- Full Text
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