ArticlePLoS biology2013
Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains.
Article in PLoS biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
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106 citing papers in PubMed, 169 citations in OpenAlex.
- Molecular Regulation of Virulence and Dental Biofilm Formation in Streptococcus mutans: Unravelling the Crosstalk Between the VicRK and LiaSR Two-Component Systems.Molecular oral microbiology · 2026Review
- Conformational diversity in poly-HAMP arrays and its implications for signal transduction.Protein science : a publication of the Protein Society · 2026Article
- Molecular basis of quorum-sensing signal transduction by CqsS and its inhibition by CqsA the autoinducer synthase.bioRxiv : the preprint server for biology · 2026Article
- Functional Characterization of the Histidine Kinase BaeS Reveals Critical Residues for BaeSR-Dependent Stress Signaling inMicroorganisms · 2026Article
- Staphylococcus aureus sensor histidine kinase VraS mutations linked to antibiotic resistance affect enzymatic catalysis, stability, and substrate interactions.Archives of biochemistry and biophysics · 2026Article
- Mutations in two-component signaling systems drive experimental evolution of tigecycline and colistin resistance inAntimicrobial agents and chemotherapy · 2025Article
- Insights Into the Conformational Dynamics of the Cytoplasmic Domain of Metal-Sensing Sensor Histidine Kinase ZraS.Proteins · 2025Article
- A Designed ZnJournal of the American Chemical Society · 2025Article
- Two-Component System Sensor Kinase Inhibitors Target the ATP-Lid of PmrB to Disrupt Colistin Resistance inBiochemistry · 2025Article
- Mechanism of sensor kinase CitA transmembrane signaling.Nature communications · 2025Article
- Mechanism of activation and autophosphorylation of a histidine kinase.Communications chemistry · 2024Article
- Kinase-catalyzed biotinylation for discovery and validation of substrates to multispecificity kinases NME1 and NME2.The Journal of biological chemistry · 2024Article
- Atomic insights into the signaling landscape of E. coli PhoQ histidine kinase from molecular dynamics simulations.Scientific reports · 2024Article
- LOV1 protein of Pseudomonas cichorii JBC1 modulates its virulence and lifestyles in response to blue light.Scientific reports · 2024Article
- Virtual Screening of Inhibitors ofACS medicinal chemistry letters · 2024Article
- Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling.Nature communications · 2024Article
- AlphaFold2 captures the conformational landscape of the HAMP signaling domain.Protein science : a publication of the Protein Society · 2024Article
- Common sense: why bacterial sensing systems are an important target for new antibiotics.Future microbiology · 2024Article
- Comparison of Phenotype Nutritional Profiles and Phosphate Metabolism Genes in Four Serovars ofMicroorganisms · 2023Article
- 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
46 more citing papers are in PubMed but not listed here.
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Authors and funding
15 authors at 4 institutions in 3 countries.
Funding
Abstract
Two-component systems (TCSs) are important for the adaptation and survival of bacteria and fungi under stress conditions. A TCS is often composed of a membrane-bound sensor histidine kinase (SK) and a response regulator (RR), which are relayed through sequential phosphorylation steps. However, the mechanism for how an SK is switched on in response to environmental stimuli remains obscure. Here, we report the crystal structure of a complete cytoplasmic portion of an SK, VicK from Streptococcus mutans. The overall structure of VicK is a long-rod dimer that anchors four connected domains: HAMP, Per-ARNT-SIM (PAS), DHp, and catalytic and ATP binding domain (CA). The HAMP, a signal transducer, and the PAS domain, major sensor, adopt canonical folds with dyad symmetry. In contrast, the dimer of the DHp and CA domains is asymmetric because of different helical bends in the DHp domain and spatial positions of the CA domains. Moreover, a conserved proline, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. Together, the elegant architecture of VicK with a signal transducer and sensor domain suggests a model where DHp helical bending and a CA swing movement are likely coordinated for autokinase activation.
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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.