Halorhodopsin, an archaeal rhodopsin ubiquitous in Haloarchaea, uses Light
energy to pump chloride through biological membranes. Halorhodopsin crystal
s were grown in a cubic Lipidic phase, which allowed the x-ray structure de
termination of this anion pump at 1.8 angstrom resolution. Halorhodopsin as
sembles to trimers around a central patch consisting of palmitic acid. Next
to the protonated Schiff base between Lys(242) and the isomerizable retina
l chromophore, a single chloride ion occupies the transport site. Energetic
calculations on chloride binding reveal a combination of ion-ion and ion-d
ipole interactions for stabilizing the anion 18 angstroms below the membran
e surface. ion dragging across the protonated Schiff base explains why chlo
ride and proton translocation modes are mechanistically equivalent in archa
eal rhodopsins.