Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A Schiff base connectivity switch in sensory rhodopsin signaling.

Proceedings of the National Academy of Sciences of the United States of America - 21 Oct 2008

Sineshchekov Oleg A, Sasaki Jun, Phillips Brian J, Spudich John L

Abstract excerpt

Sensory rhodopsin I (SRI) in Halobacterium salinarum acts as a receptor for single-quantum attractant and two-quantum repellent phototaxis, transmitting light stimuli via its bound transducer HtrI. Signal-inverting mutations in the SRI-HtrI complex reverse the single-quantum response from attractant to repellent. Fast intramolecular charge movements reported here reveal that the unphotolyzed SRI-HtrI complex...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Membrane Proteins
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Binding

Share to Protein Structure, Tertiary

Share to Schiff Bases

Share to Signal Transduction

Source

Open in PubMed Open full text

Identifiers

PMID: 18852467
DOI: 10.1073/pnas.0807486105
PMCID: PMC2571000

Genes

SRI

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A Schiff base connectivity switch in sensory rhodopsin signaling.PMID 18852467Read ↗

Suppressor mutation analysis of the sensory rhodopsin I-transducer complex: insights into the color-sensing mechanism.Semantic proximity Read ↗

Proton transport by sensory rhodopsins and its modulation by transducer-binding.Semantic proximity Read ↗

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

Five residues in the HtrI transducer membrane-proximal domain close the cytoplasmic proton-conducting channel of sensory rhodopsin I.Semantic proximity Read ↗

Different dark conformations function in color-sensitive photosignaling by the sensory rhodopsin I-HtrI complex.Semantic proximity Read ↗

Structural changes of sensory rhodopsin I and its transducer protein are dependent on the protonated state of Asp76.Semantic proximity Read ↗

General concept for ion translocation by halobacterial retinal proteins: the isomerization/switch/transfer (IST) model.Semantic proximity Read ↗

Signal relay from sensory rhodopsin I to the cognate transducer HtrI: assessing the critical change in hydrogen-bonding between Tyr-210 and Asn-53.Semantic proximity Read ↗

A microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties.Semantic proximity Read ↗

Spectral tuning in sensory rhodopsin I from Salinibacter ruber.Semantic proximity Read ↗

Structure of an Inward Proton-Transporting Anabaena Sensory Rhodopsin Mutant: Mechanistic Insights.Semantic proximity Read ↗

Electrostatic Control of Photoisomerization in Channelrhodopsin 2.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.