Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket
- Rothschild, K.J.
- Braiman, M.S.
- Mogi, T.
- Stern, L.J.
- Khorana, H.G.
Publication date
July 1989
DOI Publisher
Published by Elsevier B.V. ISSN
0014-5793 Citation count (estimate)
27Abstract
AbstractA 3-dimensional model for the retinal binding pocket in the light-driven proton pump, bacteriorhodopsin, is proposed on the basis of spectroscopic studies of bacteriorhodopsin mutants. In this model Trp-182, Pro-186 and Trp-189 surround the polyene chain while Tyr-185 is positioned close to the retinylidene Schiff base. This model is supported by sequence homologies in the F-helices of bacteriorhodopsin and the related retinal proteins, halorhodopsin and rhodopsins
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