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 and insight into blue light-induced changes in the BlrP1 BLUF domain.

Biochemistry - 31 Mar 2009

Wu Qiong, Gardner Kevin H

Abstract excerpt

BLUF domains (sensors of blue light using flavin adenine dinucleotide) are a group of flavin-containing blue light photosensory domains from a variety of bacterial and algal proteins. While spectroscopic studies have indicated that these domains reorganize their interactions with an internally bound chromophore upon illumination, it remains unclear how these are converted into structural and functional changes....

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Proteins
Share to Flavin-Adenine Dinucleotide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Klebsiella pneumoniae

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 19191473
DOI: 10.1021/bi802237r

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 and insight into blue light-induced changes in the BlrP1 BLUF domain.PMID 19191473Read ↗

Characterization of elements involved in allosteric light regulation of phosphodiesterase activity by comparison of different functional BlrP1 states.Semantic proximity Read ↗

Crystal structures of the AppA BLUF domain photoreceptor provide insights into blue light-mediated signal transduction.Semantic proximity Read ↗

Characterization of BLUF-photoreceptors present in <i>Acinetobacter nosocomialis</i>Semantic proximity Read ↗

BlsA Is a Low to Moderate Temperature Blue Light Photoreceptor in the Human Pathogen Acinetobacter baumanniiSemantic proximity Read ↗

Structure of a cyanobacterial BLUF protein, Tll0078, containing a novel FAD-binding blue light sensor domain.Semantic proximity Read ↗

Spectroscopic studies of the AppA BLUF domain from Rhodobacter sphaeroides: addressing movement of tryptophan 104 in the signaling state.Semantic proximity Read ↗

BLUF domain function does not require a metastable radical intermediate state.Semantic proximity Read ↗

Single Amino Acid Mutation Decouples Photochemistry of the BLUF Domain from the Enzymatic Function of OaPAC and Drives the Enzyme to a Switched-on State.Semantic proximity Read ↗

A Q63E Rhodobacter sphaeroides AppA BLUF domain mutant is locked in a pseudo-light-excited signaling state.Semantic proximity Read ↗

Transient IR spectroscopy identifies key interactions and unravels new intermediates in the photocycle of a bacterial phytochrome.Semantic proximity Read ↗

Conserved Signal Transduction Mechanisms and Dark Recovery Kinetic Tuning in the Pseudomonadaceae Short Light, Oxygen, Voltage (LOV) Protein Family.Semantic proximity Read ↗

The functional role of a conserved loop in EAL domain-based cyclic di-GMP-specific phosphodiesterase.Semantic proximity Read ↗

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