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Article

Tryptophan at position 104 is involved in transforming light signal into changes of beta-sheet structure for the signaling state in the BLUF domain of AppA.

Plant & cell physiology - 1 Dec 2005

Masuda Shinji, Hasegawa Koji, Ono Taka-aki

Abstract excerpt

AppA is a member of an FAD-based new class blue-light sensory protein known as sensor of blue light using FAD (BLUF) protein. The spectroscopic properties of an AppA BLUF domain (AppA126), in which the tryptophan residue at position 104 had been replaced with alanine (W104A), were characterized. The W104A mutant AppA126 showed a nearly normal absorption red shift in the FAD UV-visible absorption upon...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16204305
DOI: 10.1093/pcp/pci208

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.

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Tryptophan at position 104 is involved in transforming light signal into changes of beta-sheet structure for the signaling state in the BLUF domain of AppA.PMID 16204305Read ↗

Structural refinement of a key tryptophan residue in the BLUF photoreceptor AppA by ultraviolet resonance Raman spectroscopy.Semantic proximity Read ↗

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

Electron transfer quenching in light adapted and mutant forms of the AppA BLUF 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 ↗

The critical role of a hydrogen bond between Gln63 and Trp104 in the blue-light sensing BLUF domain that controls AppA activity.Semantic proximity Read ↗

Ultrafast structural dynamics in BLUF domains: transient infrared spectroscopy of AppA and its mutants.Semantic proximity Read ↗

Serine in BLUF domains displays spectral importance in computational models.Semantic proximity Read ↗

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

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

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Structure and insight into blue light-induced changes in the BlrP1 BLUF domain.Semantic proximity Read ↗

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