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

doi:10.1016/0014-5793(89)80774-4

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 journal › Article › peer-review

42 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 language	English (US)
Pages (from-to)	448-452
Number of pages	5
Journal	FEBS Letters
Volume	250
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(89)80774-4
State	Published - Jul 3 1989
Externally published	Yes

Keywords

Halorhodopsin
Proline
Proton transport
Rhodopsin
Tryptophan

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(89)80774-4

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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.",

keywords = "Halorhodopsin, Proline, Proton transport, Rhodopsin, Tryptophan",

author = "Rothschild, {K. J.} and Braiman, {M. S.} and T. Mogi and Stern, {L. J.} and Khorana, {H. G.}",

note = "Funding Information: Acknowledgements: This work was supported by grants from the NSF (PCM-8110992), NIH (GM-28289-06) and ONR (N00014-82-K-0668) to H.G.K. and NSF (DMB-8509587), NIH (EY-EY05499-05) and ONR (N00014-88-K-0464) to K.J.R. M.S.B. is a Lucille P. Markey Scholar and this work was supported in part by a grant from the Lucille P. Markey Charitable Trust. We wish to thank Gerald Stubbs for providing the crystallographic coordinates for TMV and Patrick Ahl, Richard Henderson, Maarten Heyn and Sriram Subramaniam for helpful discussions.",

year = "1989",

month = jul,

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doi = "10.1016/0014-5793(89)80774-4",

language = "English (US)",

volume = "250",

pages = "448--452",

journal = "FEBS Letters",

issn = "0014-5793",

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number = "2",

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T1 - Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket

AU - Rothschild, K. J.

AU - Braiman, M. S.

AU - Mogi, T.

AU - Stern, L. J.

AU - Khorana, H. G.

N1 - Funding Information: Acknowledgements: This work was supported by grants from the NSF (PCM-8110992), NIH (GM-28289-06) and ONR (N00014-82-K-0668) to H.G.K. and NSF (DMB-8509587), NIH (EY-EY05499-05) and ONR (N00014-88-K-0464) to K.J.R. M.S.B. is a Lucille P. Markey Scholar and this work was supported in part by a grant from the Lucille P. Markey Charitable Trust. We wish to thank Gerald Stubbs for providing the crystallographic coordinates for TMV and Patrick Ahl, Richard Henderson, Maarten Heyn and Sriram Subramaniam for helpful discussions.

PY - 1989/7/3

Y1 - 1989/7/3

N2 - 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.

AB - 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.

KW - Halorhodopsin

KW - Proline

KW - Proton transport

KW - Rhodopsin

KW - Tryptophan

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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