1. Crystal structure of Escherichia coli-expressed Haloarcula marismortui bacteriorhodopsin I in the trimeric form
- Author
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Shevchenko, Vitaly, Gushchin, Ivan, Polovinkin, V., Round, E., Borshchevskiy, Valentin, Utrobin, P., Popov, A., Balandin, Taras, Büldt, Georg, Gordeliy, Valentin, Moscow Inst Phys & Technol, Lab Adv Studies Membrane Prot, Dolgoprudnyi, Russia, Res Ctr Julich GmbH, Inst Complex Syst ICS Struct Biochem 6, Julich, Germany, Institut de biologie structurale (IBS - UMR 5075 ), 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)-Centre National de la Recherche Scientifique (CNRS), European Synchrotron Radiation Facility (ESRF), Institut de biologie structurale (IBS - UMR 5075), 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)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Moscow Institute of Physics and Technology [Moscow] (MIPT), Institute of Complex Systems (ICS), Forschungszentrum Jülich GmbH, Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)
- Subjects
Haloarcula marismortui ,Membrane Protein Complexes ,[SDV]Life Sciences [q-bio] ,Cell Membranes ,Biophysics ,lcsh:Medicine ,Industrial Processes ,Research and Analysis Methods ,Crystallography, X-Ray ,Biochemistry ,Protein Structure, Secondary ,Industrial Engineering ,Escherichia coli ,lcsh:Science ,Ion Transport ,lcsh:R ,Biology and Life Sciences ,Proteins ,Protein Complexes ,Membrane Proteins ,Water ,Hydrogen Bonding ,Cell Biology ,Crystallization Techniques ,Lipids ,Membrane Protein Crystallization ,Macromolecular Crystallography ,Transmembrane Proteins ,Separation Processes ,[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM] ,Bacteriorhodopsins ,Crystallographic Techniques ,Engineering and Technology ,lcsh:Q ,ddc:500 ,Cellular Structures and Organelles ,Protein Multimerization ,Hydrophobic and Hydrophilic Interactions ,Research Article - Abstract
International audience; Bacteriorhodopsins are a large family of seven-helical transmembrane proteins that function as light-driven proton pumps. Here, we present the crystal structure of a new member of the family, Haloarcula marismortui bacteriorhodopsin I (HmBRI) D94N mutant, at the resolution of 2.5 angstrom. While the HmBRI retinal-binding pocket and proton donor site are similar to those of other archaeal proton pumps, its proton release region is extended and contains additional water molecules. The protein's fold is reinforced by three novel inter-helical hydrogen bonds, two of which result from double substitutions relative to Halobacterium salinarum bacteriorhodopsin and other similar proteins. Despite the expression in Escherichia coli and consequent absence of native lipids, the protein assembles as a trimer in crystals. The unique extended loop between the helices D and E of HmBRI makes contacts with the adjacent protomer and appears to stabilize the interface. Many lipidic hydrophobic tail groups are discernible in the membrane region, and their positions are similar to those of archaeal isoprenoid lipids in the crystals of other proton pumps, isolated from native or native-like sources. All these features might explain the HmBRI properties and establish the protein as a novel model for the microbial rhodopsin proton pumping studies
- Published
- 2014