ArticleThe Journal of biological chemistry2010
Structural and enzymatic insights into the ATP binding and autophosphorylation mechanism of a sensor histidine kinase.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Article
- The accessory protein CvnF8 modulates histidine kinase activity in an Actinobacterial G protein system inbioRxiv : the preprint server for biology · 2025Article
- Allosteric coupling activation mechanism in histidine kinases.Scientific reports · 2025Article
- Article
- LiaR-dependent gene expression contributes to antimicrobial responses in group AAntimicrobial agents and chemotherapy · 2024Article
- Understanding ATP Binding to DosS Catalytic Domain with a Short ATP-Lid.Biochemistry · 2023Article
- NH125 Sensitizes Staphylococcus aureus to Cell Wall-Targeting Antibiotics through the Inhibition of the VraS Sensor Histidine Kinase.Microbiology spectrum · 2023Article
- Novel Substrates for Kinases Involved in the Biosynthesis of Inositol Pyrophosphates and Their Enhancement of ATPase Activity of a Kinase.Molecules (Basel, Switzerland) · 2021Article
- Integrated sensing of host stresses by inhibition of a cytoplasmic two-component system controlseLife · 2021Article
- Article
- Directed evolution reveals the mechanism of HitRS signaling transduction in Bacillus anthracis.PLoS pathogens · 2020Article
- Driving the catalytic activity of a transmembrane thermosensor kinase.Cellular and molecular life sciences : CMLS · 2020Article
- Phosphoregulated orthogonal signal transduction in mammalian cells.Nature communications · 2020Article
- Structural asymmetry does not indicate hemiphosphorylation in the bacterial histidine kinase CpxA.The Journal of biological chemistry · 2020Article
- Identification of Novel Thermosensors in Gram-Positive Pathogens.Frontiers in molecular biosciences · 2020Article
- The Staphylococcus aureus ArlRS two-component system regulates virulence factor expression through MgrA.Molecular microbiology · 2020Article
- Structural insights into the signalling mechanisms of two-component systems.Nature reviews. Microbiology · 2018Review
- Convergence of PASTA Kinase and Two-Component Signaling in Response to Cell Wall Stress in Enterococcus faecalis.Journal of bacteriology · 2018Article
- Probing the nucleotide-binding activity of a redox sensor: two-component regulatory control in chloroplasts.Photosynthesis research · 2016Article
- Molecular Mechanisms of Two-Component Signal Transduction.Journal of molecular biology · 2016Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DesK is a sensor histidine kinase (HK) that allows Bacillus subtilis to respond to cold shock, triggering the adaptation of membrane fluidity via transcriptional control of a fatty acid desaturase. It belongs to the HK family HPK7, which includes the nitrogen metabolism regulators NarX/Q and the antibiotic sensor LiaS among other important sensor kinases. Structural information on different HK families is still scarce and several questions remain, particularly concerning the molecular features that determine HK specificity during its catalytic autophosphorylation and subsequent response-regulator phosphotransfer reactions. To analyze the ATP-binding features of HPK7 HKs and dissect their mechanism of autophosphorylation at the molecular level, we have studied DesK in complex with ATP using high resolution structural approaches in combination with biochemical studies. We report the first crystal structure of an HK in complex with its natural nucleotidic substrate. The general fold of the ATP-binding domain of DesK is conserved, compared with well studied members of other families. Yet, DesK displays a far more compact structure at the ATP-binding pocket: the ATP lid loop is much shorter with no secondary structural organization and becomes ordered upon ATP loading. Sequence conservation mapping onto the molecular surface, semi-flexible protein-protein docking simulations, and structure-based point mutagenesis allow us to propose a specific domain-domain geometry during autophosphorylation catalysis. Supporting our hypotheses, we have been able to trap an autophosphorylating intermediate state, by protein engineering at the predicted domain-domain interaction surface.
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