Shuttling between two protein conformations: the common mechanism for sensory transduction and ion transport (Q41099727)

26 September 2017

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title

Shuttling between two protein conformations: the common mechanism for sensory transduction and ion transport (English)

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26 September 2017

Spudich JL

1

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26 September 2017

Lanyi JK

series ordinal

2

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26 September 2017

publication date

1 August 1996

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Current Opinion in Cell Biology

26 September 2017

published in

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26 September 2017

volume

8

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26 September 2017

issue

4

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26 September 2017

page(s)

452-457

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Bacteriorhodopsin as a model for proton pumps

26 September 2017

cites work

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Halorhodopsin, a light-driven electrogenic chloride-transport system

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Characterization of rhodopsin-transducin interaction: a mutant rhodopsin photoproduct with a protonated Schiff base activates transducin

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7 January 2021

Removal of the transducer protein from sensory rhodopsin I exposes sites of proton release and uptake during the receptor photocycle

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Removal of transducer HtrI allows electrogenic proton translocation by sensory rhodopsin I.

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Protein-protein interaction converts a proton pump into a sensory receptor

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The photoreceptor sensory rhodopsin I as a two-photon-driven proton pump

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Asp76 is the Schiff base counterion and proton acceptor in the proton-translocating form of sensory rhodopsin I.

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Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin

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Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle

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7 January 2021

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7 January 2021

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7 January 2021

Primary structure of an archaebacterial transducer, a methyl-accepting protein associated with sensory rhodopsin I

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7 January 2021

Signal transduction in the archaeon Halobacterium salinarium is processed through three subfamilies of 13 soluble and membrane-bound transducer proteins

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7 January 2021

The Schiff base counterion of bacteriorhodopsin is protonated in sensory rhodopsin I: spectroscopic and functional characterization of the mutated proteins D76N and D76A.

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7 January 2021

Evidence that the repellent receptor form of sensory rhodopsin I is an attractant signaling state

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7 January 2021

Mechanism of colour discrimination by a bacterial sensory rhodopsin

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Protonatable residues at the cytoplasmic end of transmembrane helix-2 in the signal transducer HtrI control photochemistry and function of sensory rhodopsin I.

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Residue replacements of buried aspartyl and related residues in sensory rhodopsin I: D201N produces inverted phototaxis signals

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7 January 2021

10.1016/S0955-0674(96)80020-2

Identifiers

DOI

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26 September 2017

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