Discover Community Create You

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

Structure of photoactive yellow protein (PYP) E46Q mutant at 1.2 A resolution suggests how Glu46 controls the spectroscopic and kinetic characteristics of PYP.

Acta crystallographica. Section D, Biological crystallography - 1 Dec 2004

Sugishima Masakazu, Tanimoto Norihiko, Soda Koji, Hamada Norio, Tokunaga Fumio, Fukuyama Keiichi

Abstract excerpt

Photoactive yellow protein from Ectothiorhodospira halophila is a photoreceptor protein involved in the negative phototaxis of this bacterium. Its chromophore (p-coumaric acid) is deprotonated in the ground state, which is stabilized by a hydrogen-bond network between Tyr42, Glu46 and Thr50. Glu46 is a key residue as it has been suggested that the proton at Glu46 is transferred to the chromophore during its...

Read the complete abstract on PubMed

Topics

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

Share to Coumaric Acids
Share to Glutamic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hot Temperature

Share to Hydrogen Bonding

Share to Models, Chemical

Share to Propionates

Share to Spectrophotometry

Share to Ultraviolet Rays

Source

Identifiers

PMID: 15583378
DOI: 10.1107/S0907444904024084

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of photoactive yellow protein (PYP) E46Q mutant at 1.2 A resolution suggests how Glu46 controls the spectroscopic and kinetic characteristics of PYP.PMID 15583378Read ↗

Functional tuning of photoactive yellow protein by active site residue 46.Semantic proximity Read ↗

Protonation/deprotonation reactions triggered by photoactivation of photoactive yellow protein from Ectothiorhodospira halophila.Semantic proximity Read ↗

Kinetics of proton uptake and dye binding by photoactive yellow protein in wild type and in the E46Q and E46A mutants.Semantic proximity Read ↗

Effect of salt and pH on the activation of photoactive yellow protein and gateway mutants Y98Q and Y98F.Semantic proximity Read ↗

Active site mutants implicate key residues for control of color and light cycle kinetics of photoactive yellow protein.Semantic proximity Read ↗

Short hydrogen bonds in photoactive yellow protein.Semantic proximity Read ↗

Strong hydrogen bond between glutamic acid 46 and chromophore leads to the intermediate spectral form and excited state proton transfer in the Y42F mutant of the photoreceptor photoactive yellow protein.Semantic proximity Read ↗

A structural pathway for signaling in the E46Q mutant of photoactive yellow protein.Semantic proximity Read ↗

Changes in the hydrogen-bond network around the chromophore of photoactive yellow protein in the ground and excited states.Semantic proximity Read ↗

Origins of the Intermediate Spectral Form in M100 Mutants of Photoactive Yellow Protein.Semantic proximity Read ↗

Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein.Semantic proximity Read ↗

Out of the blue: the photocycle of the photoactive yellow protein.Semantic proximity Read ↗

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