globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1915888117
论文题名:
High-resolution structural insights into the heliorhodopsin family
作者: Kovalev K.; Volkov D.; Astashkin R.; Alekseev A.; Gushchin I.; Haro-Moreno J.M.; Chizhov I.; Siletsky S.; Mamedov M.; Rogachev A.; Balandin T.; Borshchevskiy V.; Popov A.; Bourenkov G.; Bamberg E.; Rodriguez-Valera F.; Büldt G.; Gordeliy V.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2020
卷: 117, 期:8
起始页码: 4131
结束页码: 4141
语种: 英语
英文关键词: Crystal structure ; Membrane protein ; Retinal ; Rhodopsin ; X-ray crystallography
Scopus关键词: amino acid ; heliorhodopsin ; membrane protein ; rhodopsin ; Schiff base ; unclassified drug ; rhodopsin ; Article ; bacterial strain ; biological phenomena and functions concerning the entire organism ; cluster analysis ; cytoplasm ; dimerization ; enzyme activity ; hydrophobicity ; nonhuman ; pH ; priority journal ; protein analysis ; protein expression ; protein family ; protein function ; protein purification ; protein structure ; structural bioinformatics ; biology ; chemistry ; molecular model ; photolysis ; protein conformation ; Computational Biology ; Hydrogen-Ion Concentration ; Models, Molecular ; Photolysis ; Protein Conformation ; Rhodopsins, Microbial
英文摘要: Rhodopsins are the most abundant light-harvesting proteins. A new family of rhodopsins, heliorhodopsins (HeRs), has recently been discovered. Unlike in the known rhodopsins, in HeRs the N termini face the cytoplasm. The function of HeRs remains unknown. We present the structures of the bacterial HeR-48C12 in two states at the resolution of 1.5 Å, which highlight its remarkable difference from all known rhodopsins. The interior of HeR’s extracellular part is completely hydrophobic, while the cytoplasmic part comprises a cavity (Schiff base cavity [SBC]) surrounded by charged amino acids and containing a cluster of water molecules, presumably being a primary proton acceptor from the Schiff base. At acidic pH, a planar triangular molecule (acetate) is present in the SBC. Structure-based bioinformatic analysis identified 10 subfamilies of HeRs, suggesting their diverse biological functions. The structures and available data suggest an enzymatic activity of HeR-48C12 subfamily and their possible involvement in fundamental redox biological processes. © 2020 National Academy of Sciences. All rights reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/164319
Appears in Collections:气候变化与战略

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作者单位: Kovalev, K., Institut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-Commission for Atomic Energy (CEA)-CNRS, Grenoble, 38000, France, Institute of Biological Information Processing (Institute of Biological Information Processing: Structural Biochemistry), Forschungszentrum Jülich, Jülich, 52428, Germany, Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, 52428, Germany, Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation, Institute of Crystallography, University of Aachen (Rheinisch-Westfälische Technische Hochschule Aachen [RWTH]), Aachen, 52062, Germany; Volkov, D., Institute of Biological Information Processing (Institute of Biological Information Processing: Structural Biochemistry), Forschungszentrum Jülich, Jülich, 52428, Germany, Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, 52428, Germany; Astashkin, R., Institut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-Commission for Atomic Energy (CEA)-CNRS, Grenoble, 38000, France, Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation; Alekseev, A., Institute of Biological Information Processing (Institute of Biological Information Processing: Structural Biochemistry), Forschungszentrum Jülich, Jülich, 52428, Germany, Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, 52428, Germany, Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation, Institute of Crystallography, University of Aachen (Rheinisch-Westfälische Technische Hochschule Aachen [RWTH]), Aachen, 52062, Germany; Gushchin, I., Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation; Haro-Moreno, J.M., Evolutionary Genomics Group, Departamento de Producción Vegetal y Microbiología, Universidad Miguel Hernández, 03202, San Juan de Alicante, Spain; Chizhov, I., Institute for Biophysical Chemistry, Hannover Medical School, Hannover, 30625, Germany; Siletsky, S., Belozersky Institute of Physical-Chemical Biology, Lomonosov Moscow State University, Moscow, 119234, Russian Federation; Mamedov, M., Belozersky Institute of Physical-Chemical Biology, Lomonosov Moscow State University, Moscow, 119234, Russian Federation; Rogachev, A., Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation, Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research, Dubna, 141980, Russian Federation; Balandin, T., Institute of Biological Information Processing (Institute of Biological Information Processing: Structural Biochemistry), Forschungszentrum Jülich, Jülich, 52428, Germany, Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, 52428, Germany; Borshchevskiy, V., Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation; Popov, A., Structural Biology Group, European Synchrotron Radiation Facility, Grenoble, 38000, France; Bourenkov, G., Hamburg Unit care of Deutsches Elektronen-Synchrotron (DESY), European Molecular Biology Laboratory, Hamburg, 22607, Germany; Bamberg, E., Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation, Biophysical Chemistry, Max Planck Institute of Biophysics, Frankfurt am Main, 60438, Germany; Rodriguez-Valera, F., Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation, Evolutionary Genomics Group, Departamento de Producción Vegetal y Microbiología, Universidad Miguel Hernández, 03202, San Juan de Alicante, Spain; Büldt, G., Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation; Gordeliy, V., Institut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-Commission for Atomic Energy (CEA)-CNRS, Grenoble, 38000, France, Institute of Biological Information Processing (Institute of Biological Information Processing: Structural Biochemistry), Forschungszentrum Jülich, Jülich, 52428, Germany, Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, 52428, Germany, Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation

Recommended Citation:
Kovalev K.,Volkov D.,Astashkin R.,et al. High-resolution structural insights into the heliorhodopsin family[J]. Proceedings of the National Academy of Sciences of the United States of America,2020-01-01,117(8)
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