A three-dimensional movie of structural changes in bacteriorhodopsin

• Autores: Eriko Nango, Antoine Royant
• Localización: Science, ISSN 0036-8075, Vol. 354, Nº 6319, 2016, págs. 1552-1557
• Idioma: inglés
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• Resumen

  • 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.