Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket.
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.
Rothschild
K J
KJ
Department of Physics, Boston University, MA 02215.
Braiman
M S
MS
Mogi
T
T
Stern
L J
LJ
Khorana
H G
HG
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
C020932:11-cis-retinal-binding protein; D000596:Amino Acids; D002352:Carrier Proteins; D025602:Halorhodopsins; D001436:Bacteriorhodopsins; D012243:Rhodopsin