doi: 10.1016/0014-5793(89)80774-4.
Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket
Affiliations
- PMID: 2753143
- DOI: 10.1016/0014-5793(89)80774-4
Item in Clipboard
Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket
FEBS Lett.
.
Free article
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.
Similar articles
-
Substitution of amino acids in helix F of bacteriorhodopsin: effects on the photochemical cycle.Biochemistry. 1989 Dec 26;28(26):10028-34. doi: 10.1021/bi00452a022. Biochemistry. 1989. PMID: 2575916
-
Asp76 is the Schiff base counterion and proton acceptor in the proton-translocating form of sensory rhodopsin I.Biochemistry. 1996 May 28;35(21):6690-6. doi: 10.1021/bi9600355. Biochemistry. 1996. PMID: 8639619
-
Analogies between halorhodopsin and bacteriorhodopsin.Biochim Biophys Acta. 2000 Aug 30;1460(1):220-9. doi: 10.1016/s0005-2728(00)00141-9. Biochim Biophys Acta. 2000. PMID: 10984602 Review.
-
Comparative studies on ion pumps of the bacterial rhodopsin family.Biophys Chem. 1994 May;50(1-2):191-201. doi: 10.1016/0301-4622(94)85031-3. Biophys Chem. 1994. PMID: 8011934 Review.
-
Conformational changes in sensory rhodopsin I: similarities and differences with bacteriorhodopsin, halorhodopsin, and rhodopsin.Biochemistry. 1991 Jun 4;30(22):5395-400. doi: 10.1021/bi00236a010. Biochemistry. 1991. PMID: 2036407
Cited by
-
FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model.J Bioenerg Biomembr. 1992 Apr;24(2):147-67. doi: 10.1007/BF00762674. J Bioenerg Biomembr. 1992. PMID: 1526959 Review.
-
Effects of tryptophan mutation on the deprotonation and reprotonation kinetics of the Schiff base during the photocycle of bacteriorhodopsin.Biophys J. 1992 May;61(5):1281-8. doi: 10.1016/S0006-3495(92)81936-7. Biophys J. 1992. PMID: 1318094 Free PMC article.
-
Quantum efficiency of the photochemical cycle of bacteriorhodopsin.Biophys J. 1990 Sep;58(3):597-608. doi: 10.1016/S0006-3495(90)82403-6. Biophys J. 1990. PMID: 19431766 Free PMC article.
-
Hydration dependence of active core fluctuations in bacteriorhodopsin.Biophys J. 2008 Jul;95(1):194-202. doi: 10.1529/biophysj.107.120386. Epub 2008 Mar 13. Biophys J. 2008. PMID: 18339747 Free PMC article.
-
Photoactivation of rhodopsin involves alterations in cysteine side chains: detection of an S-H band in the Meta I-->Meta II FTIR difference spectrum.Biophys J. 1994 Jun;66(6):2085-91. doi: 10.1016/S0006-3495(94)81003-3. Biophys J. 1994. PMID: 8075342 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
