A three-dimensional movie of structural changes in bacteriorhodopsin-Reference-Cited by-同舟云学术

A three-dimensional movie of structural changes in bacteriorhodopsin

Published:2016-12-23 Issue:6319 Volume:354 Page:1552-1557
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Nango Eriko¹²,Royant Antoine³⁴,Kubo Minoru¹⁵,Nakane Takanori⁶,Wickstrand Cecilia⁷,Kimura Tetsunari¹⁸,Tanaka Tomoyuki¹,Tono Kensuke⁹,Song Changyong¹¹⁰,Tanaka Rie¹,Arima Toshi¹,Yamashita Ayumi¹,Kobayashi Jun¹,Hosaka Toshiaki¹¹,Mizohata Eiichi¹²,Nogly Przemyslaw¹³,Sugahara Michihiro¹,Nam Daewoong¹⁰,Nomura Takashi¹,Shimamura Tatsuro²,Im Dohyun²,Fujiwara Takaaki²,Yamanaka Yasuaki²,Jeon Byeonghyun¹⁰,Nishizawa Tomohiro⁵⁶,Oda Kazumasa⁶,Fukuda Masahiro⁶,Andersson Rebecka⁷,Båth Petra⁷,Dods Robert⁷,Davidsson Jan¹⁴,Matsuoka Shigeru¹⁵,Kawatake Satoshi¹⁵,Murata Michio¹⁵,Nureki Osamu⁶,Owada Shigeki¹,Kameshima Takashi⁹,Hatsui Takaki¹,Joti Yasumasa⁹,Schertler Gebhard¹³¹⁶,Yabashi Makina¹,Bondar Ana-Nicoleta¹⁷,Standfuss Jörg¹³,Neutze Richard⁷,Iwata So¹²

Affiliation:

1. RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.

2. Department of Cell Biology, Graduate School of Medicine, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.

3. Université Grenoble Alpes, CNRS, Commissariat à l’Energie Atomique et aux Energies Alternatives, Institut de Biologie Structurale, F-38044 Grenoble, France.

4. European Synchrotron Radiation Facility, F-38043 Grenoble, France.

5. Japan Science and Technology Agency (JST)–Precursory Research for Embryonic Science and Technology (PRESTO), 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan.

6. Department of Biological Sciences, Graduate School of Science, University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.

7. Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.

8. Department of Chemistry, Graduate School of Science, Kobe University, 1-1 Rokkodai, Nada-ku, Kobe 657-8501, Japan.

9. Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.

10. Department of Physics, Pohang University of Science and Technology, Pohang 790-784, Korea.

11. Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.

12. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.

13. Division of Biology and Chemistry, Laboratory for Biomolecular Research, Paul Scherrer Institute, 5232 Villigen, Switzerland.

14. Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.

15. JST–Exploratory Research for Advanced Technology (ERATO), Lipid Active Structure Project, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.

16. Department of Biology, ETH Zurich, 8093 Zürich, Switzerland.

17. Theoretical Molecular Biophysics, Department of Physics, Freie Universität Berlin, Arnimallee 14, D-14195 Berlin, Germany.

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

Funder

Swedish Research Council

Swedish Foundation for Strategic Research

Knut and Alice Wallenberg Foundation

French National Research Agency

Japan Society for the Promotion of Science KAKENHI

European Community’s Seventh Framework Program

Swiss National Science Foundation

NCCR-MUST/FAST

National Research Foundation of Korea

POSCO Green Science

Freie Universität Berlin