Asymmetric structure of the purple membrane.

Abstract

There is both functional and structural evidence that bacteriorhodopsin is oriented asymmetrically across the purple membrane of Halobacterium halobium. To assess the degree of asymmetry, the x-ray diffraction data from the membrane have been analyzed for possible electron-density profiles. A recent theory predicts that only a limited number of profiles are consistent with the continuous diffraction data, and two possible profiles have been found. Both profiles indicate that the protein molecules span a lipid bilayer in the membrane. Both profiles are asymmetric; there are more lipid molecules in one half of the membrane than in the other, and the bacteriorhodopsin molecule shows a slight complementary asymmetry.