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 |
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Pages (from-to) | 1552-1557 |
Number of pages | 6 |
Journal | Science |
Volume | 354 |
Issue number | 6319 |
DOIs | |
Publication status | Published - 2016 Dec 23 |
Externally published | Yes |
ASJC Scopus subject areas
- General