Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 A resolution.

@article{Belrhali1999ProteinLA,
  title={Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 A resolution.},
  author={Hassan Belrhali and Peter Nollert and Antoine Royant and Christoph Menzel and J{\"u}rg P. Rosenbusch and Ehud M. Landau and Eva Pebay-Peyroula},
  journal={Structure},
  year={1999},
  volume={7 8},
  pages={909-17}
}
BACKGROUND Bacteriorhodopsin (bR) from Halobacterium salinarum is a proton pump that converts the energy of light into a proton gradient that drives ATP synthesis. The protein comprises seven transmembrane helices and in vivo is organized into purple patches, in which bR and lipids form a crystalline two-dimensional array. Upon absorption of a photon, retinal, which is covalently bound to Lys216 via a Schiff base, is isomerized to a 13-cis,15-anti configuration. This initiates a sequence of… CONTINUE READING
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