ArticleNature communications2017
Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
50 citing papers in PubMed, 79 citations in OpenAlex.
- Sequential structural changes in the monomeric LOV histidine kinase EL346 revealed by transient infrared spectroscopy.Physical chemistry chemical physics : PCCP · 2026Article
- A light-triggered Time-Resolved X-ray Solution Scattering (TR-XSS) workflow with application to protein conformational dynamics.FEBS open bio · 2026Article
- Real-time Structural Tracking of Slow P-type ATPase Dynamics.The Journal of membrane biology · 2026Article
- Dimer asymmetry in signaling of blue light sensor histidine kinases.Science advances · 2026Article
- Assessing protein-specific radiation damage in time-resolved X-ray solution-scattering experiments at high-brilliance synchrotrons using fast detector readout.Acta crystallographica. Section D, Structural biology · 2026Article
- A novel two-component system regulates shikimate pathway for thermal adaptation in Thermus thermophilus.Nucleic acids research · 2026Article
- Signal propagation in LOV-based multidomain proteins: time-resolved infrared spectroscopy reveals the complete photocycle of YF1 and PAL.Physical chemistry chemical physics : PCCP · 2026Article
- Framework for Quantifying the Efficiency of Competing Signal Transmission Modes in Proteins.Journal of the American Chemical Society · 2026Article
- Insights Into the Conformational Dynamics of the Cytoplasmic Domain of Metal-Sensing Sensor Histidine Kinase ZraS.Proteins · 2025Article
- Small Protein Domains as Potential Spin Labels for In Vitro, Cellular, and Light-Induced Dipolar EPR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Variations in kinase and effector signaling logic in a bacterial two component signaling network.The Journal of biological chemistry · 2025Article
- Variations in kinase and effector signaling logic in a bacterial two component signaling network.bioRxiv : the preprint server for biology · 2025Article
- Two-Component System Sensor Kinase Inhibitors Target the ATP-Lid of PmrB to Disrupt Colistin Resistance inBiochemistry · 2025Article
- Time-resolved X-ray solution scattering unveils the events leading to hemoglobin heme capture by staphylococcal IsdB.Nature communications · 2025Article
- Microsecond time-resolved X-ray scattering by utilizing MHz repetition rate at second-generation XFELs.Nature methods · 2024Article
- Structural dynamics of protein-protein association involved in the light-induced transition of Avena sativa LOV2 protein.Nature communications · 2024Article
- Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling.Nature communications · 2024Article
- Photoacoustic Calorimetry Studies of OBiochemistry · 2024Article
- Structural insights into redox signal transduction mechanisms in the control of nitrogen fixation by the NifLA system.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Reaction dynamics studiedChemical science · 2022Review
Corrections and comments
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Authors and funding
20 authors at 9 institutions in 6 countries.
Funding
Abstract
Sensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use nano- to millisecond time-resolved X-ray scattering to visualize the solution structural changes that occur when the light-sensitive model histidine kinase YF1 is activated by blue light. We find that the coiled coil linker and the attached histidine kinase domains undergo a left handed rotation within microseconds. In a much slower second step, the kinase domains rearrange internally. This structural mechanism presents a template for signal transduction in sensor histidine kinases.Sensor histidine kinases (SHK) consist of sensor, linker and kinase modules and different models for SHK signal transduction have been proposed. Here the authors present nano- to millisecond time-resolved X-ray scattering measurements, which reveal a structural mechanism for kinase domain activation in SHK.
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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.