A three-dimensionalmovie of structural changes in bacteriorhodopsin

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

doi:10.1126/science.aah3497

A three-dimensionalmovie of structural changes in bacteriorhodopsin

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

Research output: Contribution to journal › Article › peer-review

252 Citations (Scopus)

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 watermolecule 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.

Original language	English
Pages (from-to)	1552-1557
Number of pages	6
Journal	Science
Volume	354
Issue number	6319
DOIs	https://doi.org/10.1126/science.aah3497
Publication status	Published - 2016 Dec 23
Externally published	Yes

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Nango, E., Royant, A., Kubo, M., Nakane, T., Wickstrand, C., Kimura, T., Tanaka, T., Tono, K., Song, C., Tanaka, R., Arima, T., Yamashita, A., Kobayashi, J., Hosaka, T., Mizohata, E., Nogly, P., Sugahara, M., Nam, D., Nomura, T., ... Iwata, S. (2016). A three-dimensionalmovie of structural changes in bacteriorhodopsin. Science, 354(6319), 1552-1557. https://doi.org/10.1126/science.aah3497

A three-dimensionalmovie of structural changes in bacteriorhodopsin. / Nango, Eriko; Royant, Antoine; Kubo, Minoru; Nakane, Takanori; Wickstrand, Cecilia; Kimura, Tetsunari; Tanaka, Tomoyuki; Tono, Kensuke; Song, Changyong; 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.

In: Science, Vol. 354, No. 6319, 23.12.2016, p. 1552-1557.

Research output: Contribution to journal › Article › peer-review

Nango, E, Royant, A, Kubo, M, Nakane, T, Wickstrand, C, Kimura, T, Tanaka, T, Tono, K, Song, C, Tanaka, R, Arima, T, Yamashita, A, Kobayashi, J, Hosaka, T, Mizohata, E, Nogly, P, Sugahara, M, Nam, D, Nomura, T, Shimamura, T, Im, D, Fujiwara, T, Yamanaka, Y, Jeon, B, Nishizawa, T, Oda, K, Fukuda, M, Andersson, R, Båth, P, Dods, R, Davidsson, J, Matsuoka, S, Kawatake, S, Murata, M, Nureki, O, Owada, S, Kameshima, T, Hatsui, T, Joti, Y, Schertler, G, Yabashi, M, Bondar, AN, Standfuss, J, Neutze, R & Iwata, S 2016, 'A three-dimensionalmovie of structural changes in bacteriorhodopsin', Science, vol. 354, no. 6319, pp. 1552-1557. https://doi.org/10.1126/science.aah3497

Nango, Eriko ; Royant, Antoine ; Kubo, Minoru ; Nakane, Takanori ; Wickstrand, Cecilia ; Kimura, Tetsunari ; Tanaka, Tomoyuki ; Tono, Kensuke ; Song, Changyong ; 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. / A three-dimensionalmovie of structural changes in bacteriorhodopsin. In: Science. 2016 ; Vol. 354, No. 6319. pp. 1552-1557.

@article{e3e632ce23fe4fa1b3279670c9f1ba34,

title = "A three-dimensionalmovie of structural changes in bacteriorhodopsin",

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 watermolecule 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.",

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

note = "Funding Information: This work was supported by the X-ray Free-Electron Laser Priority Strategy Program (Ministry of Education, Culture, Sports, Science and Technology of Japan) and partially by the Strategic Basic Research Program (JST) and RIKEN Pioneering Project Dynamic Structural Biology. We acknowledge computational support from the SACLA High Performance Computing system and the Mini-K supercomputer system. R.N. acknowledges financial support from the Swedish Research Council (grants VR 349-2011-6485 and 2015-00560), the Swedish Foundation for Strategic Research (grant SSF SRL 10-0036), and the Knut and Alice Wallenberg Foundation (grant KAW 2012.0284). A.R. acknowledges financial support from the French National Research Agency (grant ANR-11-JSV5-0009). T.Ki. is supported by Japan Society for the Promotion of Science KAKENHI grant 15H05476. P.N. acknowledges support from the European Community's Seventh Framework Program (FP7/2007-2013) under grant 290605 (PSI-FELLOW/COFUND). J.S. acknowledges support from the Swiss National Science Foundation project grant (SNF 31003A-159558). G.S. acknowledges support from the Swiss National Science Foundation (grant SNF 310030-153145) and the NCCR-MUST/FAST program. C.S. is supported by National Research Foundation of Korea (grants NRF-2015R1A5A1009962 and NRF-2016R1A2B3010980) and the POSCO Green Science program. Publisher Copyright: {\textcopyright}2016 by the American Association for the Advancement of Science; all rights reserved.",

year = "2016",

month = dec,

day = "23",

doi = "10.1126/science.aah3497",

language = "English",

volume = "354",

pages = "1552--1557",

journal = "Science",

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T1 - A three-dimensionalmovie of structural changes in bacteriorhodopsin

AU - Nango, Eriko

AU - Royant, Antoine

AU - Kubo, Minoru

AU - Nakane, Takanori

AU - Wickstrand, Cecilia

AU - Kimura, Tetsunari

AU - Tanaka, Tomoyuki

AU - Tono, Kensuke

AU - Song, Changyong

AU - Tanaka, Rie

AU - Arima, Toshi

AU - Yamashita, Ayumi

AU - Kobayashi, Jun

AU - Hosaka, Toshiaki

AU - Mizohata, Eiichi

AU - Nogly, Przemyslaw

AU - Sugahara, Michihiro

AU - Nam, Daewoong

AU - Nomura, Takashi

AU - Shimamura, Tatsuro

AU - Im, Dohyun

AU - Fujiwara, Takaaki

AU - Yamanaka, Yasuaki

AU - Jeon, Byeonghyun

AU - Nishizawa, Tomohiro

AU - Oda, Kazumasa

AU - Fukuda, Masahiro

AU - Andersson, Rebecka

AU - Båth, Petra

AU - Dods, Robert

AU - Davidsson, Jan

AU - Matsuoka, Shigeru

AU - Kawatake, Satoshi

AU - Murata, Michio

AU - Nureki, Osamu

AU - Owada, Shigeki

AU - Kameshima, Takashi

AU - Hatsui, Takaki

AU - Joti, Yasumasa

AU - Schertler, Gebhard

AU - Yabashi, Makina

AU - Bondar, Ana Nicoleta

AU - Standfuss, Jörg

AU - Neutze, Richard

AU - Iwata, So

N1 - Funding Information: This work was supported by the X-ray Free-Electron Laser Priority Strategy Program (Ministry of Education, Culture, Sports, Science and Technology of Japan) and partially by the Strategic Basic Research Program (JST) and RIKEN Pioneering Project Dynamic Structural Biology. We acknowledge computational support from the SACLA High Performance Computing system and the Mini-K supercomputer system. R.N. acknowledges financial support from the Swedish Research Council (grants VR 349-2011-6485 and 2015-00560), the Swedish Foundation for Strategic Research (grant SSF SRL 10-0036), and the Knut and Alice Wallenberg Foundation (grant KAW 2012.0284). A.R. acknowledges financial support from the French National Research Agency (grant ANR-11-JSV5-0009). T.Ki. is supported by Japan Society for the Promotion of Science KAKENHI grant 15H05476. P.N. acknowledges support from the European Community's Seventh Framework Program (FP7/2007-2013) under grant 290605 (PSI-FELLOW/COFUND). J.S. acknowledges support from the Swiss National Science Foundation project grant (SNF 31003A-159558). G.S. acknowledges support from the Swiss National Science Foundation (grant SNF 310030-153145) and the NCCR-MUST/FAST program. C.S. is supported by National Research Foundation of Korea (grants NRF-2015R1A5A1009962 and NRF-2016R1A2B3010980) and the POSCO Green Science program. Publisher Copyright: ©2016 by the American Association for the Advancement of Science; all rights reserved.

PY - 2016/12/23

Y1 - 2016/12/23

N2 - 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 watermolecule 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.

AB - 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 watermolecule 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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DO - 10.1126/science.aah3497

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VL - 354

SP - 1552

EP - 1557

JO - Science

JF - Science

SN - 0036-8075

IS - 6319

ER -

A three-dimensionalmovie of structural changes in bacteriorhodopsin

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