| Literature DB >> 28008064 |
Eriko Nango1,2, Antoine Royant3,4, Minoru Kubo1,5, Takanori Nakane6, Cecilia Wickstrand7, Tetsunari Kimura1,8, Tomoyuki Tanaka1, Kensuke Tono9, Changyong Song1,10, Rie Tanaka1, Toshi Arima1, Ayumi Yamashita1, Jun Kobayashi1, Toshiaki Hosaka11, Eiichi Mizohata12, Przemyslaw Nogly13, Michihiro Sugahara1, Daewoong Nam10, Takashi Nomura1, Tatsuro Shimamura2, Dohyun Im2, Takaaki Fujiwara2, Yasuaki Yamanaka2, Byeonghyun Jeon10, Tomohiro Nishizawa5,6, Kazumasa Oda6, Masahiro Fukuda6, Rebecka Andersson7, Petra Båth7, Robert Dods7, Jan Davidsson14, Shigeru Matsuoka15, Satoshi Kawatake15, Michio Murata15, Osamu Nureki6, Shigeki Owada1, Takashi Kameshima9, Takaki Hatsui1, Yasumasa Joti9, Gebhard Schertler13,16, Makina Yabashi1, Ana-Nicoleta Bondar17, Jörg Standfuss13, Richard Neutze18, So Iwata19,2.
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.Entities:
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Year: 2016 PMID： 28008064 DOI： 10.1126/science.aah3497
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728