Journal
SCIENCE
Volume 354, Issue 6319, Pages 1552-1557Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aah3497
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Funding
- X-ray Free-Electron Laser Priority Strategy Program (Ministry of Education, Culture, Sports, Science and Technology of Japan)
- Strategic Basic Research Program (JST)
- RIKEN Pioneering Project Dynamic Structural Biology
- Swedish Research Council [VR 349-2011-6485, 2015-00560]
- Swedish Foundation for Strategic Research [SSF SRL 10-0036]
- Knut and Alice Wallenberg Foundation [KAW 2012.0284]
- French National Research Agency [ANR-11-JSV5-0009]
- Japan Society for the Promotion of Science KAKENHI [15H05476]
- European Community's Seventh Framework Program [290605]
- Swiss National Science Foundation [SNF 31003A_159558, SNF 310030_153145]
- NCCR-MUST/FAST program
- National Research Foundation of Korea [NRF-2015R1A5A1009962, NRF-2016R1A2B3010980]
- POSCO Green Science program
- Excellence Initiative of the German Federal Government via the Freie Universitat Berlin
- Excellence Initiative of the German State Government via the Freie Universitat Berlin
- Deutsche Forschungsgemeinschaft (DFG) through the Collaborative Research Center [SFB1078]
- Exploratory Research for Advanced Technology of the JST
- National Research Foundation of Korea [2016R1A2B3010980] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- Grants-in-Aid for Scientific Research [15H01055, 15K18523, 16H06315, 15H04338, 15H05476] Funding Source: KAKEN
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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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