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

Mutational effects on protein structural changes and interdomain interactions in the blue-light sensing LOV protein YtvA.

Photochemistry and photobiology - 1 Jan 2000

Losi Aba, Ghiraldelli Elisa, Jansen Sven, Gärtner Wolfgang

Abstract excerpt

Mutagenesis studies on the phototropin-related protein YtvA from Bacillus subtilis have revealed the role of selected structural elements in interdomain communication. The LOV (light, oxygen, voltage) domain of YtvA undergoes light-driven reactions similar to that of phot-LOV, with reversible formation of a covalent flavin-cysteine adduct. The mutated proteins Ytva-E105L and YtvA-E56Q have been studied by UV...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Base Sequence

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Protein Structure, Tertiary

Share to Spectrum Analysis

Source

Identifiers

PMID: 16022561
DOI: 10.1562/2005-05-25-RA-541

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

Mutational effects on protein structural changes and interdomain interactions in the blue-light sensing LOV protein YtvA.PMID 16022561Read ↗

Interdomain signalling in the blue-light sensing and GTP-binding protein YtvA: a mutagenesis study uncovering the importance of specific protein sites.Semantic proximity Read ↗

The amino acids surrounding the flavin 7a-methyl group determine the UVA spectral features of a LOV protein.Semantic proximity Read ↗

NTP-binding properties of the blue-light receptor YtvA and effects of the E105L mutation.Semantic proximity Read ↗

Effect of tryptophan mutation on the structure of LOV1 domain of phototropin1 protein of Ostreococcus tauri: A combined molecular dynamics simulation and biophysical approach.Semantic proximity Read ↗

A conserved isoleucine in the LOV1 domain of a novel phototropin from the marine alga Ostreococcus tauri modulates the dark state recovery of the domain.Semantic proximity Read ↗

Mechanism-based tuning of a LOV domain photoreceptor.Semantic proximity Read ↗

The photocycle of a flavin-binding domain of the blue light photoreceptor phototropin.Semantic proximity Read ↗

Residue alterations within a conserved hydrophobic pocket influence light, oxygen, voltage photoreceptor dark recovery.Semantic proximity Read ↗

In vivo mutational analysis of YtvA from Bacillus subtilis: mechanism of light activation of the general stress response.Semantic proximity Read ↗

Switching from adduct formation to electron transfer in a light-oxygen-voltage domain containing the reactive cysteine.Semantic proximity Read ↗

Signals of LOV1: a computer simulation study on the wildtype LOV1-domain of Chlamydomonas reinhardtii and its mutants.Semantic proximity Read ↗

Unusual photodynamic characteristics of the light-oxygen-voltage domain of phototropin linked to terrestrial adaptation of Klebsormidium nitens.Semantic proximity Read ↗

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