1. Active State of Sensory Rhodopsin II: Structural Determinants for Signal Transfer and Proton Pumping
- Author
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Martin Engelhard, Anastasia Reshetnyak, Valentin Gordeliy, Andrii Ishchenko, Sergei Grudinin, Valentin Borshchevskiy, Ekaterina Round, Ivan Gushchin, Georg Büldt, Moscow Institute of Physics and Technology [Moscow] (MIPT), Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institute of Complex Systems (ICS), Forschungszentrum Jülich GmbH | Centre de recherche de Juliers, Helmholtz-Gemeinschaft = Helmholtz Association-Helmholtz-Gemeinschaft = Helmholtz Association, Institute of Crystallography [Aachen], Rheinisch-Westfälische Technische Hochschule Aachen University (RWTH), Algorithms for Modeling and Simulation of Nanosystems (NANO-D), Inria Grenoble - Rhône-Alpes, Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-Laboratoire Jean Kuntzmann (LJK), Université Pierre Mendès France - Grenoble 2 (UPMF)-Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Centre National de la Recherche Scientifique (CNRS)-Université Pierre Mendès France - Grenoble 2 (UPMF)-Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Centre National de la Recherche Scientifique (CNRS), Max Planck Institute of Molecular Physiology, Max-Planck-Gesellschaft, This work was supported by the program 'Chaires d'excellence' edition 2008 of ANR France, by a CEA(IBS)-HGF(FZJ) STC 5.1 specific agreement, and by a Marie Curie grant for the training and career development of researchers (FP7-PEOPLE- 2007-1-1-ITN, project SBMPs). This work was performed in the framework of Russian State contract numbers 02.740.11.0299, 02.740.11.5010, 974 (in the framework of activity 1.2.2), and P211 (in the framework of activity 1.3.2) of the Federal Target Program 'Scientific and academic research cadres of innovative Russia' for the years 2009- 2013., European Project: 211800,EC:FP7:PEOPLE,FP7-PEOPLE-2007-1-1-ITN,SBMPS(2008), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Rheinisch-Westfälische Technische Hochschule Aachen (RWTH), and Centre National de la Recherche Scientifique (CNRS)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Université Joseph Fourier - Grenoble 1 (UJF)-Université Pierre Mendès France - Grenoble 2 (UPMF)-Centre National de la Recherche Scientifique (CNRS)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Université Joseph Fourier - Grenoble 1 (UJF)-Université Pierre Mendès France - Grenoble 2 (UPMF)
- Subjects
Models, Molecular ,Protein Folding ,Archaeal Proteins ,Natronobacterium ,[PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph] ,Crystallography, X-Ray ,Models, Biological ,Signal ,03 medical and health sciences ,Structural Biology ,Sensory Rhodopsins ,membrane protein ,Molecular Biology ,030304 developmental biology ,G protein-coupled receptor ,0303 health sciences ,Halobacteriaceae ,[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] ,biology ,Chemistry ,030302 biochemistry & molecular biology ,Sensory rhodopsin II ,Proton Pumps ,Carotenoids ,Transmembrane protein ,Protein Structure, Tertiary ,Transport protein ,Crystallography ,active state ,Rhodopsin ,Biophysics ,biology.protein ,Bacterial rhodopsins ,Signal transduction ,Crystallization ,signaling ,Signal Transduction ,bacterial rhodopsins - Abstract
International audience; The molecular mechanism of transmembrane signal transduction is still a pertinent question in cellular biology. Generally, a receptor can transfer an external signal via its cytoplasmic surface as found for GPCRs like rhodopsin or via the membrane domain like it is utilized by sensory rhodopsin II (SRII) in complex with its transducer HtrII. In the absence of HtrII SRII functions as a proton pump. Here, we report on the crystal structure of the active state of SRII from Natronomonas pharaonis (NpSRII). The problem of a dramatic loss of the diffraction quality upon loading of the active state was overcome by growing better crystals and reducing the occupancy of the state. The determined conformational changes at the region comprising helices F and G are similar to those observed for the NpSRII-transducer complex but they are much more pronounced. Meaning of these differences for proton pumping ability and understanding of the signal transduction by NpSRII is discussed.
- Published
- 2011
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