ArticleThe Journal of biological chemistry
Structural basis of KdpD histidine kinase binding to the second messenger c-di-AMP.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- The NmpRSTU multi-component signaling system ofJournal of bacteriology · 2025Article
- In silico biotechnological potential of Bacillus sp. strain MHSD_37 bacterial endophyte.BMC genomics · 2024Article
- KdpD is a tandem serine histidine kinase that controls KNature communications · 2024Article
- In Silico Analysis of Changes in Predicted Metabolic Capabilities of Intestinal Microbiota after Fecal Microbial Transplantation for Treatment of RecurrentMicroorganisms · 2023Article
- Universal Stress Proteins: From Gene to Function.International journal of molecular sciences · 2023Review
- c-di-AMP signaling is required for bile salt resistance, osmotolerance, and long-term host colonization byScience signaling · 2022Article
- Transcriptomic and Metabolomic Analysis of a Fusidic Acid-SelectedAntibiotics (Basel, Switzerland) · 2022Article
- An RNA-binding protein acts as a major post-transcriptional modulator in Bacillus anthracis.Nature communications · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The KdpDE two-component system regulates potassium homeostasis and virulence in various bacterial species. The KdpD histidine kinases (HK) of this system contain a universal stress protein (USP) domain which binds to the second messenger cyclic-di-adenosine monophosphate (c-di-AMP) for regulating transcriptional output from this two-component system in Firmicutes such as Staphylococcus aureus. However, the structural basis of c-di-AMP specificity within the KdpD-USP domain is not well understood. Here, we resolved a 2.3 Å crystal structure of the S. aureus KdpD-USP domain (USP
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Registered trials
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