ArticleThe Journal of biological chemistry2015
Structural Studies of Potassium Transport Protein KtrA Regulator of Conductance of K+ (RCK) C Domain in Complex with Cyclic Diadenosine Monophosphate (c-di-AMP).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Cyclic di-AMP signaling and regulation inmSphere · 2026Review
- Cyclic di-adenosine monophosphate as a potential regulator of sporulation and solventogenesis in Clostridium beijerinckii: a hypothesis.World journal of microbiology & biotechnology · 2026Review
- Regulation of potassium homeostasis inFrontiers in microbiology · 2026Article
- The second messenger signaling molecule cyclic di-AMP drives developmental cycle progression ineLife · 2025Article
- TrkA ofMicrobiology (Reading, England) · 2025Article
- Cyclic di-AMP alleviates periodontitis by activating PI3K/Akt/Nrf2 pathways.Frontiers in cellular and infection microbiology · 2025Article
- Article
- Bacterial cell volume regulation and the importance of cyclic di-AMP.Microbiology and molecular biology reviews : MMBR · 2024Review
- Structural basis and synergism of ATP and NaNature communications · 2024Article
- Allosteric regulation by c-di-AMP modulates a complete N-acetylglucosamine signaling cascade in Saccharopolyspora erythraea.Nature communications · 2024Article
- c-di-AMP determines the hierarchical organization of bacterial RCK proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Temporal control of Staphylococcus aureus intracellular pH by sodium and potassium.FEMS microbiology letters · 2024Article
- Structural insights into the regulation, ligand recognition, and oligomerization of bacterial STING.Nature communications · 2023Article
- Nucleotides as Bacterial Second Messengers.Molecules (Basel, Switzerland) · 2023Review
- Cyclic di-AMP traps proton-coupled KNature communications · 2023Article
- Redundant potassium transporter systems guarantee the survival ofFrontiers in microbiology · 2023Article
- Putative nucleotide-based second messengers in archaea.microLife · 2023Review
- Loss of GdpP Function in Staphylococcus aureus Leads to β-Lactam Tolerance and Enhanced Evolution of β-Lactam Resistance.Antimicrobial agents and chemotherapy · 2022Article
- c-di-AMP Accumulation Regulates Growth, Metabolism, and Immunogenicity ofFrontiers in microbiology · 2022Article
- BusR senses bipartite DNA binding motifs by a unique molecular ruler architecture.Nucleic acids research · 2021Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although it was only recently identified as a second messenger, c-di-AMP was found to have fundamental importance in numerous bacterial functions such as ion transport. The potassium transporter protein, KtrA, was identified as a c-di-AMP receptor. However, the co-crystallization of c-di-AMP with the protein has not been studied. Here, we determined the crystal structure of the KtrA RCK_C domain in complex with c-di-AMP. The c-di-AMP nucleotide, which adopts a U-shaped conformation, is bound at the dimer interface of RCK_C close to helices α3 and α4. c-di-AMP interacts with KtrA RCK_C mainly by forming hydrogen bonds and hydrophobic interactions. c-di-AMP binding induces the contraction of the dimer, bringing the two monomers of KtrA RCK_C into close proximity. The KtrA RCK_C was able to interact with only c-di-AMP, but not with c-di-GMP, 3',3-cGAMP, ATP, and ADP. The structure of the KtrA RCK_C domain and c-di-AMP complex would expand our understanding about the mechanism of inactivation in Ktr transporters governed by c-di-AMP.
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