ArticleBiochemistry2005
Structure of a novel photoreceptor, the BLUF domain of AppA from Rhodobacter sphaeroides.
Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed.
- Probing the Signal Transduction Mechanism of the Light-Activated Adenylate Cyclase OaPAC Using Unnatural Amino Acid Mutagenesis.ACS chemical biology · 2025Article
- Enhancing Proton-Coupled Electron Transfer in Blue Light Using FAD Photoreceptor AppAJournal of the American Chemical Society · 2025Article
- Unveiling the Photoactivation Mechanism of BLUF Photoreceptor Protein through Hybrid Quantum Mechanics/Molecular Mechanics Free-Energy Calculation.ACS physical chemistry Au · 2024Article
- Article
- 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.Journal of molecular biology · 2024Article
- Origin of the multi-phasic quenching dynamics in the BLUF domains across the species.Nature communications · 2024Article
- Optical Approaches for Investigating Neuromodulation and G Protein-Coupled Receptor Signaling.Pharmacological reviews · 2023Review
- pH-Dependent Binding and Releasing Mechanism of Acetate in the Inner Water Cavity of Heliorhodopsin.Biochemistry · 2023Article
- Gas and light: triggers of c-di-GMP-mediated regulation.FEMS microbiology reviews · 2023Review
- Integrated Computational Study of the Light-Activated Structure of the AppA BLUF Domain and Its Spectral Signatures.The journal of physical chemistry. A · 2023Article
- Fast Method for Excited-State Dynamics in Complex Systems and Its Application to the Photoactivation of a Blue Light Using Flavin Photoreceptor.The journal of physical chemistry letters · 2023Article
- Spectroscopic and Computational Observation of Glutamine Tautomerization in the Blue Light Sensing Using Flavin Domain Photoreaction.Journal of the American Chemical Society · 2023Article
- Proton transfer and conformational changes along the hydrogen bond network in heliorhodopsin.Communications biology · 2022Article
- Unraveling the Photoactivation Mechanism of a Light-Activated Adenylyl Cyclase Using Ultrafast Spectroscopy Coupled with Unnatural Amino Acid Mutagenesis.ACS chemical biology · 2022Article
- The nature of proton-coupled electron transfer in a blue light using flavin domain.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural Analyses of CrtJ and Its BMicroorganisms · 2022Article
- Time-resolved diffusion reveals photoreactions of BLUF proteins with similar functional domains.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Review
- From crystallographic data to the solution structure of photoreceptors: the case of the AppA BLUF domain.Chemical science · 2021Article
- Ultrafast Transient Infrared Spectroscopy of Photoreceptors with Polarizable QM/MM Dynamics.The journal of physical chemistry. B · 2021Article
- Peripheral Methionine Residues Impact Flavin Photoreduction and Protonation in an Engineered LOV Domain Light Sensor.Biochemistry · 2021Article
9 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
Abstract
The flavin-binding BLUF domain of AppA represents a new class of blue light photoreceptors that are present in a number of bacterial and algal species. The dark state X-ray structure of this domain was determined at 2.3 A resolution. The domain demonstrates a new function for the common ferredoxin-like fold; two long alpha-helices flank the flavin, which is bound with its isoalloxazine ring perpendicular to a five-stranded beta-sheet. The hydrogen bond network and the overall protein topology of the BLUF domain (but not its sequence) bear some resemblance to LOV domains, a subset of PAS domains widely involved in signaling. Nearly all residues conserved in BLUF domains surround the flavin chromophore, many of which are involved in an intricate hydrogen bond network. Photoactivation may induce a rearrangement in this network via reorientation of the Gln63 side chain to form a new hydrogen bond to the flavin O4 position. This shift would also break a hydrogen bond to the Trp104 side chain, which may be critical in induction of global structural change in AppA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.