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A three-dimensional movie of structural changes in bacteriorhodopsin

Authors :
Eriko Nango
Jörg Standfuss
Shigeki Owada
Takanori Nakane
Petra Båth
Robert Dods
Ayumi Yamashita
Byeonghyun Jeon
Minoru Kubo
Takaaki Fujiwara
Jan Davidsson
Rebecka Andersson
Dohyun Im
Michihiro Sugahara
Yasuaki Yamanaka
Kazumasa Oda
Makina Yabashi
Osamu Nureki
Takaki Hatsui
Kensuke Tono
Tomoyuki Tanaka
Michio Murata
Gebhard F. X. Schertler
Antoine Royant
Daewoong Nam
Takashi Nomura
Eiichi Mizohata
Satoshi Kawatake
Tetsunari Kimura
So Iwata
Przemyslaw Nogly
Tatsuro Shimamura
Takashi Kameshima
Changyong Song
Masahiro Fukuda
Jun Kobayashi
Shigeru Matsuoka
Yasumasa Joti
Ana-Nicoleta Bondar
Richard Neutze
Cecilia Wickstrand
Toshiaki Hosaka
Rie Tanaka
Toshi Arima
Tomohiro Nishizawa
RIKEN - Institute of Physical and Chemical Research [Japon] (RIKEN)
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)
Department of Biological Sciences
The University of Tokyo (UTokyo)
Department of Chemistry and Molecular Biology [Gothenburg]
University of Gothenburg (GU)
Division of Structural and Synthetic Biology
RIKEN Center for Life Science Technologies (RIKEN CLST)
RIKEN - Institute of Physical and Chemical Research [Japon] (RIKEN)-RIKEN - Institute of Physical and Chemical Research [Japon] (RIKEN)
Department of Applied Chemistry
Osaka University [Osaka]
Division of Biology and Chemistry, Laboratory for Biomolecular Research
Paul Scherrer Institute (PSI)
Institut Armand Frappier (INRS-IAF)
Institut National de la Recherche Scientifique [Québec] (INRS)-Réseau International des Instituts Pasteur (RIIP)
Department of Physics
Pohang University of Science and Technology (POSTECH)
Department of Cell Biology, Graduate School of Medicine
Kyoto University [Kyoto]
Angström Laboratory
Uppsala University
JST-Exploratory Research for Advanced Technology (ERATO)
Japan Synchrotron Radiation Research Institute [Hyogo] (JASRI)
Theoretical Molecular Biophysics, Department of Physics
Freie Universität Berlin
ANR-11-JSV5-0009,SOxygen,Oxygène singulet : du dégât sur les protéines vers le développement de bio-détecteurs et générateurs(2011)
Centre National de la Recherche Scientifique (CNRS)-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)
Kyoto University
Source :
Science, Science, American Association for the Advancement of Science, 2016, 354 (6319), pp.1552-1557. ⟨10.1126/science.aah3497⟩, Science, 2016, 354 (6319), pp.1552-1557. ⟨10.1126/science.aah3497⟩
Publication Year :
2016
Publisher :
HAL CCSD, 2016.

Abstract

Snapshots of bacteriorhodopsin Bacteriorhodopsin is a membrane protein that harvests the energy content from light to transport protons out of the cell against a transmembrane potential. Nango et al. used timeresolved serial femtosecond crystallography at an x-ray free electron laser to provide 13 structural snapshots of the conformational changes that occur in the nanoseconds to milliseconds after photoactivation. These changes begin at the active site, propagate toward the extracellular side of the protein, and mediate internal protonation exchanges that achieve proton transport. Science , this issue p. 1552

Details

Language :
English
ISSN :
00368075 and 10959203
Database :
OpenAIRE
Journal :
Science, Science, American Association for the Advancement of Science, 2016, 354 (6319), pp.1552-1557. ⟨10.1126/science.aah3497⟩, Science, 2016, 354 (6319), pp.1552-1557. ⟨10.1126/science.aah3497⟩
Accession number :
edsair.doi.dedup.....34ff6203187afd15f42f16cdf767fb68