A three-dimensional movie of structural changes in bacteriorhodopsin

Eriko Nango(Kyoto University), Antoine Royant(Centre National de la Recherche Scientifique), Minoru Kubo(Japan Science and Technology Agency), Takanori Nakane(Tokyo University of Science), Cecilia Wickstrand(University of Gothenburg), Tetsunari Kimura(SPring-8), Tomoyuki Tanaka(SPring-8), Kensuke Tono(Japan Synchrotron Radiation Research Institute), Changyong Song(Pohang University of Science and Technology), Rie Tanaka(SPring-8), Toshi Arima(SPring-8), A. Yamashita(SPring-8), Jun Kobayashi(SPring-8), Toshiaki Hosaka, Eiichi Mizohata(The University of Osaka), Przemysław Nogły(Paul Scherrer Institute), Michihiro Sugahara(SPring-8), Daewoong Nam(Pohang University of Science and Technology), Takashi Nomura(SPring-8), Tatsuro Shimamura(Kyoto University), Dohyun Im(Kyoto University), Takaaki Fujiwara(Kyoto University), Yasuaki Yamanaka(Kyoto University), Byeonghyun Jeon(Pohang University of Science and Technology), Tomohiro Nishizawa(Tokyo University of Science), Kazumasa Oda(Tokyo University of Science), Masahiro Fukuda(Tokyo University of Science), Rebecka Andersson(University of Gothenburg), Petra Båth(University of Gothenburg), Robert Dods(University of Gothenburg), Jan Davidsson(Uppsala University), Shigeru Matsuoka(The University of Osaka), Satoshi Kawatake(The University of Osaka), Michio Murata(The University of Osaka), Osamu Nureki(Tokyo University of Science), Shigeki Owada(SPring-8), Takashi Kameshima(Japan Synchrotron Radiation Research Institute), Takaki Hatsui(SPring-8), Yasumasa Joti(Japan Synchrotron Radiation Research Institute), Gebhard F. X. Schertler(Paul Scherrer Institute), Makina Yabashi(SPring-8), Ana‐Nicoleta Bondar(Freie Universität Berlin), Jörg Standfuss(Paul Scherrer Institute), Richard Neutze(University of Gothenburg), So Iwata(Kyoto University)
Science
December 22, 2016
Cited by 436Open Access
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Abstract

Bacteriorhodopsin (bR) is a light-driven proton pump and a model membrane transport protein. We used time-resolved serial femtosecond crystallography at an x-ray free electron laser to visualize conformational changes in bR from nanoseconds to milliseconds following photoactivation. An initially twisted retinal chromophore displaces a conserved tryptophan residue of transmembrane helix F on the cytoplasmic side of the protein while dislodging a key water molecule on the extracellular side. The resulting cascade of structural changes throughout the protein shows how motions are choreographed as bR transports protons uphill against a transmembrane concentration gradient.


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