Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping.

Binding Sites Escherichia coli Protein Conformation Proton Pumps / chemistry Rhodopsins, Microbial / chemistry
X-ray crystallography proton pump rhodopsin

Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
06 04 2021
Historique:
entrez: 1 4 2021
pubmed: 2 4 2021
medline: 19 11 2021
Statut: ppublish

Résumé

Schizorhodopsins (SzRs), a new rhodopsin family identified in Asgard archaea, are phylogenetically located at an intermediate position between type-1 microbial rhodopsins and heliorhodopsins. SzRs work as light-driven inward H

Identifiants

DOI: 10.1073/pnas.2016328118 PMID: 33790007 PMC: PMC8040798
pubmed: 33790007
pii: 2016328118
doi: 10.1073/pnas.2016328118
pmc: PMC8040798
pii:
doi:

Substances chimiques

Proton Pumps 0
Rhodopsins, Microbial 0

Types de publication

Comparative Study Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

Copyright © 2021 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

The authors declare no competing interest.

Références

Nature. 2006 Jan 5;439(7072):109-12
pubmed: 16280982
Curr Protoc Bioinformatics. 2016 Jun 20;54:5.6.1-5.6.37
pubmed: 27322406
Nat New Biol. 1971 Sep 29;233(39):149-52
pubmed: 4940442
Sci Adv. 2017 Sep 22;3(9):e1603187
pubmed: 28948217
Annu Rev Biochem. 2017 Jun 20;86:845-872
pubmed: 28301742
Nat Commun. 2015 May 15;6:7177
pubmed: 25975962
Chem Rev. 2014 Jan 8;114(1):126-63
pubmed: 24364740
Nat Commun. 2016 Nov 17;7:13415
pubmed: 27853152
Nat Commun. 2019 Apr 30;10(1):1993
pubmed: 31040285
Nat Commun. 2020 Nov 5;11(1):5605
pubmed: 33154353
Biochem Biophys Res Commun. 2020 Dec 10;533(3):262-267
pubmed: 32951839
J Phys Chem Lett. 2018 Nov 15;9(22):6431-6436
pubmed: 30351947
J Biol Chem. 2004 Apr 16;279(16):16403-9
pubmed: 14757760
Nat Commun. 2013;4:1678
pubmed: 23575682
J Phys Chem B. 2020 Jun 18;124(24):4851-4872
pubmed: 32436389
Biochemistry. 2010 Apr 20;49(15):3343-50
pubmed: 20230053
Annu Rev Biophys Biomol Struct. 2000;29:291-325
pubmed: 10940251
Biochem Biophys Res Commun. 1977 Sep 9;78(1):237-43
pubmed: 20882
J Biol Chem. 1982 Sep 10;257(17):10306-13
pubmed: 7107607
J Mol Biol. 1993 Dec 5;234(3):779-815
pubmed: 8254673
Sci Adv. 2020 Apr 10;6(15):eaaz2441
pubmed: 32300653
Biochim Biophys Acta. 2001 Dec 1;1515(2):92-100
pubmed: 11718665
Science. 2018 Jul 13;361(6398):
pubmed: 29903883
J Phys Chem B. 2019 Mar 21;123(11):2507-2512
pubmed: 30742768
Biophys J. 1996 Jan;70(1):473-81
pubmed: 8770224
Acta Crystallogr D Struct Biol. 2018 May 1;74(Pt 5):441-449
pubmed: 29717715
Nature. 2020 Feb;578(7795):432-436
pubmed: 31968354
Nature. 2019 Oct;574(7776):132-136
pubmed: 31554965
Phys Chem Chem Phys. 2018 Jan 31;20(5):3165-3171
pubmed: 28975940
Nat Microbiol. 2019 Jul;4(7):1129-1137
pubmed: 30936485
Proc Natl Acad Sci U S A. 1989 Jul;86(13):4943-7
pubmed: 2544884
J Phys Chem B. 2018 Jun 28;122(25):6453-6461
pubmed: 29807427
Microbiol Mol Biol Rev. 2016 Sep 14;80(4):929-54
pubmed: 27630250
Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):352-67
pubmed: 22505256
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
pubmed: 15572765
Nature. 2020 Jan;577(7791):519-525
pubmed: 31942073
Nature. 2018 Jun;558(7711):595-599
pubmed: 29925949
Photochem Photobiol. 2017 Nov;93(6):1381-1387
pubmed: 28380687
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32
pubmed: 20124692
Science. 2016 Dec 23;354(6319):1552-1557
pubmed: 28008064
Biophys J. 1992 Mar;61(3):820-6
pubmed: 1504253
Protein Sci. 1998 Apr;7(4):1029-38
pubmed: 9568909
Science. 2019 Jul 5;365(6448):61-65
pubmed: 31273117
Protein Sci. 2000 Sep;9(9):1753-73
pubmed: 11045621
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
pubmed: 19461840
Proc Natl Acad Sci U S A. 2020 Feb 25;117(8):4131-4141
pubmed: 32034096
Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6873-7
pubmed: 1650486
J Mol Biol. 2002 Aug 23;321(4):715-26
pubmed: 12206785

Auteurs

Akimitsu Higuchi (A)

Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo 113-0033, Japan.

Wataru Shihoya (W)

Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo 113-0033, Japan; wtrshh9@gmail.com inoue@issp.u-tokyo.ac.jp nureki@bs.s.u-tokyo.ac.jp.
ORCID: 0000-0003-4813-5740

Masae Konno (M)

The Institute for Solid State Physics, The University of Tokyo, 277-8581 Kashiwa, Japan.
Precursory Research for Embryonic Science and Technology, Japan Science and Technology Agency, 4-1-8 Honcho, Saitama, 332-0012 Kawaguchi, Japan.
ORCID: 0000-0002-0605-1816

Tatsuya Ikuta (T)

Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo 113-0033, Japan.
ORCID: 0000-0002-8597-0609

Hideki Kandori (H)

Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa, 466-8555 Nagoya, Japan.
OptoBioTechnology Research Center, Nagoya Institute of Technology, Showa, 466-8555 Nagoya, Japan.

Keiichi Inoue (K)

The Institute for Solid State Physics, The University of Tokyo, 277-8581 Kashiwa, Japan; wtrshh9@gmail.com inoue@issp.u-tokyo.ac.jp nureki@bs.s.u-tokyo.ac.jp.
ORCID: 0000-0002-6898-4347

Osamu Nureki (O)

Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo 113-0033, Japan; wtrshh9@gmail.com inoue@issp.u-tokyo.ac.jp nureki@bs.s.u-tokyo.ac.jp.
ORCID: 0000-0003-1813-7008

Articles similaires

Membrane potential stimulates ADP import and ATP export by the mitochondrial ADP/ATP carrier due to its positively charged binding site.

Vasiliki Mavridou, Martin S King, Andre Bazzone et al.
1.00
Adenosine Triphosphate Adenosine Diphosphate Mitochondrial ADP, ATP Translocases Binding Sites Mitochondria

Conservation of the cooling agent binding pocket within the TRPM subfamily.

Kate Huffer, Matthew C S Denley, Elisabeth V Oskoui et al.
1.00
TRPM Cation Channels Animals Binding Sites Mice Pyrimidinones

Bioinspired gelated cell sheet-supported lactobacillus biofilm for aerobic vaginitis diagnosis and treatment.

Yueyue Gui, Qingfei Sun, Kexin Li et al.
1.00
Female Biofilms Animals Lactobacillus Mice

A head-to-head comparison of MM/PBSA and MM/GBSA in predicting binding affinities for the CB

Mei Qian Yau, Clarence W Y Liew, Jing Hen Toh et al.
1.00
Receptor, Cannabinoid, CB1 Ligands Molecular Dynamics Simulation Protein Binding Thermodynamics

Classifications MeSH

questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Sites de fixation › Crystal structure of schizorhodopsin reveals...
questionsmedicales.fr › Bactéries › Proteobacteria › Gammaproteobacteria › Enterobacteriaceae › Escherichia › Escherichia coli › Crystal structure of schizorhodopsin reveals...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Crystal structure of schizorhodopsin reveals...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines de transport membranaire › Pompes ioniques › Transporteurs de cations › Pompes à protons › Crystal structure of schizorhodopsin reveals...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Photorécepteurs microbiens › Rhodopsines microbiennes › Crystal structure of schizorhodopsin reveals...