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A three-dimensional movie of structural changes in bacteriorhodopsin.

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Nango, Eriko | Royant, Antoine | Kubo, Minoru | Nakane, Takanori | Wickstrand, Cecilia | Kimura, Tetsunari | Tanaka, Tomoyuki | Tono, Kensuke | Song, So | Tanaka, Rie | Arima, Toshi | Yamashita, Ayumi | Kobayashi, Jun | Hosaka, Toshiaki | Mizohata, Eiichi | Nogly, Przemyslaw | Sugahara, Michihiro | Nam, Daewoong | Nomura, Takashi | Shimamura, Tatsuro | Im, Dohyun | Fujiwara, Takaaki | Yamanaka, Yasuaki | Jeon, Byeonghyun | Nishizawa, Tomohiro | Oda, Kazumasa | Fukuda, Masahiro | Andersson, Rebecka | Båth, Petra | Dods, Robert | Davidsson, Jan | Matsuoka, Shigeru | Kawatake, Satoshi | Murata, Michio | Nureki, Osamu | Owada, Shigeki | Kameshima, Takashi | Hatsui, Takaki | Joti, Yasumasa | Schertler, Gebhard | Yabashi, Makina | Bondar, Ana-Nicoleta | Standfuss, Jörg | Neutze, Richard | Iwata, So

Edité par CCSD ; American Association for the Advancement of Science (AAAS) -

International audience. 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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