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Article Dans Une Revue Science Année : 2016

A three-dimensional movie of structural changes in bacteriorhodopsin.

Osamu Nureki

Résumé

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.

Dates et versions

hal-01437084 , version 1 (17-01-2017)

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Eriko Nango, Antoine Royant, Minoru Kubo, Takanori Nakane, Cecilia Wickstrand, et al.. A three-dimensional movie of structural changes in bacteriorhodopsin.. Science, 2016, 354 (6319), pp.1552-1557. ⟨10.1126/science.aah3497⟩. ⟨hal-01437084⟩
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