title: Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket.
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.
authors.affiliation: Department of Physics, Boston University, MA 02215.
authors.forename: K J
authors.initials: KJ
authors.lastname: Rothschild
authors.forename: M S
authors.initials: MS
authors.lastname: Braiman
authors.forename: T
authors.initials: T
authors.lastname: Mogi
authors.forename: L J
authors.initials: LJ
authors.lastname: Stern
authors.forename: H G
authors.initials: HG
authors.lastname: Khorana
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D001436:Bacteriorhodopsins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism; D005583:Fourier Analysis; D025602:Halorhodopsins; D011487:Protein Conformation; D012243:Rhodopsin / Q000378:metabolism; D013055:Spectrophotometry, Infrared
chemical_list: C020932:11-cis-retinal-binding protein; D000596:Amino Acids; D002352:Carrier Proteins; D025602:Halorhodopsins; D001436:Bacteriorhodopsins; D012243:Rhodopsin