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Conserved Amino Acids in F-helix of Bacteriorhodopsin Form Part of a Retinal Binding Pocket

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Journal FEBS Lett
Specialty Biochemistry
Date 1989 Jul 3
PMID 2753143
Citations 17
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Abstract

A 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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