High-resolution structural insights into the heliorhodopsin family

被引:57
作者
Kovalev, K. [1 ,2 ,3 ,4 ,5 ]
Volkov, D. [2 ,3 ]
Astashkin, R. [1 ,4 ]
Alekseev, A. [2 ,3 ,4 ,5 ]
Gushchin, I. [4 ]
Haro-Moreno, J. M. [6 ]
Chizhov, I. [7 ]
Siletsky, S. [8 ]
Mamedov, M. [8 ]
Rogachev, A. [4 ,9 ]
Balandin, T. [2 ,3 ]
Borshchevskiy, V. [4 ]
Popov, A. [10 ]
Bourenkov, G. [11 ]
Bamberg, E. [4 ,12 ]
Rodriguez-Valera, F. [4 ]
Buldt, G. [4 ]
Gordeliy, V. [1 ,2 ,3 ,4 ]
机构
[1] Univ Grenoble Alpes, CNRS, Commiss Atom Energy CEA, Inst Biol Struct JP Ebel, F-38000 Grenoble, France
[2] Forschungszentrum Julich, Inst Biol Informat Proc, Inst Biol Informat Proc Struct Biochem, D-52428 Julich, Germany
[3] Forschungszentrum Julich, JuStruct Julich Ctr Struct Biol, D-52428 Julich, Germany
[4] Natl Res Univ, Moscow Inst Phys & Technol, Res Ctr Mech Aging & Age Related Dis, Dolgoprudnyi 141701, Russia
[5] Univ Aachen, Rheinisch Westfal TH Aachen RWTH, Inst Crystallog, D-52062 Aachen, Germany
[6] Univ Miguel Hernandez, Dept Prod Vegetal & Microbiol, Evolutionary Genom Grp, Alacant 03202, Spain
[7] Hannover Med Sch, Inst Biophys Chem, D-30625 Hannover, Germany
[8] Lomonosov Moscow State Univ, Belozersky Inst Phys Chem Biol, Moscow 119234, Russia
[9] Joint Inst Nucl Res, Frank Lab Neutron Phys, Dubna 141980, Russia
[10] European Synchrotron Radiat Facil, Structural Biol Grp, F-38000 Grenoble, France
[11] Deutsch Elektronen Synchrotron DESY, European Mol Biol Lab, Hamburg Unit Care, D-22607 Hamburg, Germany
[12] Max Planck Inst Biophys, Biophys Chem, D-60438 Frankfurt, Germany
基金
俄罗斯科学基金会; 俄罗斯基础研究基金会;
关键词
rhodopsin; membrane protein; X-ray crystallography; crystal structure; retinal; SENSORY RHODOPSIN-II; RETINAL PROTEIN; WEB SERVER; RNA GENES; LIGHT; IDENTIFICATION; MEMBRANE; CHANNELRHODOPSIN-2; PROTEORHODOPSIN; PHOTOTROPHY;
D O I
10.1073/pnas.1915888117
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
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 angstrom, 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.
引用
收藏
页码:4131 / 4141
页数:11
相关论文
共 72 条
  • [1] PHENIX: a comprehensive Python']Python-based system for macromolecular structure solution
    Adams, Paul D.
    Afonine, Pavel V.
    Bunkoczi, Gabor
    Chen, Vincent B.
    Davis, Ian W.
    Echols, Nathaniel
    Headd, Jeffrey J.
    Hung, Li-Wei
    Kapral, Gary J.
    Grosse-Kunstleve, Ralf W.
    McCoy, Airlie J.
    Moriarty, Nigel W.
    Oeffner, Robert
    Read, Randy J.
    Richardson, David C.
    Richardson, Jane S.
    Terwilliger, Thomas C.
    Zwart, Peter H.
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2010, 66 : 213 - 221
  • [2] Microbial rhodopsins in the spotlight
    Bamann, Christian
    Nagel, Georg
    Bamberg, Ernst
    [J]. CURRENT OPINION IN NEUROBIOLOGY, 2010, 20 (05) : 610 - 616
  • [3] Bacterial rhodopsin:: Evidence for a new type of phototrophy in the sea
    Béjà, O
    Aravind, L
    Koonin, EV
    Suzuki, MT
    Hadd, A
    Nguyen, LP
    Jovanovich, S
    Gates, CM
    Feldman, RA
    Spudich, JL
    Spudich, EN
    DeLong, EF
    [J]. SCIENCE, 2000, 289 (5486) : 1902 - 1906
  • [4] Proteorhodopsin phototrophy in the ocean
    Béjà, O
    Spudich, EN
    Spudich, JL
    Leclerc, M
    DeLong, EF
    [J]. NATURE, 2001, 411 (6839) : 786 - 789
  • [5] Nature's toolkit for microbial rhodopsin ion pumps
    Beja, Oded
    Lanyi, Janos K.
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2014, 111 (18) : 6538 - 6539
  • [6] A eukaryotic protein, NOP-1, binds retinal to form an archaeal rhodopsin-like photochemically reactive pigment
    Bieszke, JA
    Spudich, EN
    Scott, KL
    Borkovich, KA
    Spudich, JL
    [J]. BIOCHEMISTRY, 1999, 38 (43) : 14138 - 14145
  • [7] Millisecond-timescale, genetically targeted optical control of neural activity
    Boyden, ES
    Zhang, F
    Bamberg, E
    Nagel, G
    Deisseroth, K
    [J]. NATURE NEUROSCIENCE, 2005, 8 (09) : 1263 - 1268
  • [8] Unique structure and function of viral rhodopsins
    Bratanov, Dmitry
    Kovalev, Kirill
    Machtens, Jan-Philipp
    Astashkin, Roman
    Chizhov, Igor
    Soloviov, Dmytro
    Volkov, Dmytro
    Polovinkin, Vitaly
    Zabelskii, Dmitrii
    Mager, Thomas
    Gushchin, Ivan
    Rokitskaya, Tatyana
    Antonenko, Yuri
    Alekseev, Alexey
    Shevchenko, Vitaly
    Yutin, Natalya
    Rosselli, Riccardo
    Baeken, Christian
    Borshchevskiy, Valentin
    Bourenkov, Gleb
    Popov, Alexander
    Balandin, Taras
    Buldt, Georg
    Manstein, Dietmar J.
    Rodriguez-Valera, Francisco
    Fahlke, Christoph
    Bamberg, Ernst
    Koonin, Eugene
    Gordeliy, Valentin
    [J]. NATURE COMMUNICATIONS, 2019, 10 (1)
  • [9] Fast and sensitive protein alignment using DIAMOND
    Buchfink, Benjamin
    Xie, Chao
    Huson, Daniel H.
    [J]. NATURE METHODS, 2015, 12 (01) : 59 - 60
  • [10] The photophobic receptor from Natronobacterium pharaonis:: Temperature and pH dependencies of the photocycle of sensory rhodopsin II
    Chizhov, I
    Schmies, G
    Seidel, R
    Sydor, JR
    Lüttenberg, B
    Engelhard, M
    [J]. BIOPHYSICAL JOURNAL, 1998, 75 (02) : 999 - 1009