ArticleThe Journal of biological chemistry2015
Complex structure and biochemical characterization of the Staphylococcus aureus cyclic diadenylate monophosphate (c-di-AMP)-binding protein PstA, the founding member of a new signal transduction protein family.
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 37 papers.
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Who cites it
37 citing papers in PubMed.
- A c-di-AMP-controlled glutamine synthesis pathway promotes persistence ofbioRxiv : the preprint server for biology · 2026Article
- Cyclic di-AMP inhibitsmBio · 2026Article
- Activation of a Secondary-Messenger Receptor via Allosteric Modulation of a Dynamic Conformational Ensemble.Angewandte Chemie (International ed. in English) · 2025Article
- The role ofJournal of bacteriology · 2024Article
- DarA-the central processing unit for the integration of osmotic with potassium and amino acid homeostasis inJournal of bacteriology · 2024Article
- Bacterial cell volume regulation and the importance of cyclic di-AMP.Microbiology and molecular biology reviews : MMBR · 2024Review
- Structural insights into the regulation, ligand recognition, and oligomerization of bacterial STING.Nature communications · 2023Article
- Cyclic di-AMP, a multifaceted regulator of central metabolism and osmolyte homeostasis inmicroLife · 2023Review
- Diurnal metabolic control in cyanobacteria requires perception of second messenger signaling molecule c-di-AMP by the carbon control protein SbtB.Science advances · 2021Article
- The Many Roles of the Bacterial Second Messenger Cyclic di-AMP in Adapting to Stress Cues.Journal of bacteriology · 2020Review
- A decade of research on the second messenger c-di-AMP.FEMS microbiology reviews · 2020Review
- The World of Cyclic Dinucleotides in Bacterial Behavior.Molecules (Basel, Switzerland) · 2020Review
- Cyclic di-AMP, a second messenger of primary importance: tertiary structures and binding mechanisms.Nucleic acids research · 2020Review
- c-di-AMP assists osmoadaptation by regulating theThe Journal of biological chemistry · 2019Article
- Genome-wide screen identifies novel genes required for Borrelia burgdorferi survival in its Ixodes tick vector.PLoS pathogens · 2019Article
- Increased Intracellular Cyclic di-AMP Levels Sensitize Streptococcus gallolyticus subsp. gallolyticus to Osmotic Stress and Reduce Biofilm Formation and Adherence on Intestinal Cells.Journal of bacteriology · 2019Article
- Article
- Cyclic di-adenosine monophosphate (c-di-AMP) is required for osmotic regulation inThe Journal of biological chemistry · 2018Article
- Computational and NMR spectroscopy insights into the conformation of cyclic di-nucleotides.Scientific reports · 2017Article
- Structural and functional studies of pyruvate carboxylase regulation by cyclic di-AMP in lactic acid bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
5 authors.
Funding
Abstract
Signaling nucleotides are integral parts of signal transduction systems allowing bacteria to cope with and rapidly respond to changes in the environment. The Staphylococcus aureus PII-like signal transduction protein PstA was recently identified as a cyclic diadenylate monophosphate (c-di-AMP)-binding protein. Here, we present the crystal structures of the apo- and c-di-AMP-bound PstA protein, which is trimeric in solution as well as in the crystals. The structures combined with detailed bioinformatics analysis revealed that the protein belongs to a new family of proteins with a similar core fold but with distinct features to classical PII proteins, which usually function in nitrogen metabolism pathways in bacteria. The complex structure revealed three identical c-di-AMP-binding sites per trimer with each binding site at a monomer-monomer interface. Although distinctly different from other cyclic-di-nucleotide-binding sites, as the half-binding sites are not symmetrical, the complex structure also highlighted common features for c-di-AMP-binding sites. A comparison between the apo and complex structures revealed a series of conformational changes that result in the ordering of two anti-parallel β-strands that protrude from each monomer and allowed us to propose a mechanism on how the PstA protein functions as a signaling transduction protein.
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