Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket

K. J. Rothschild, M. S. Braiman, T. Mogi, L. J. Stern, H. G. Khorana

Research output: Contribution to journalArticle

35 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)448-452
Number of pages5
JournalFEBS Letters
Volume250
Issue number2
DOIs
StatePublished - Jul 3 1989

Keywords

  • Halorhodopsin
  • Proline
  • Proton transport
  • Rhodopsin
  • Tryptophan

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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