ArticleThe EMBO journal2005
Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 140 citations in OpenAlex.
- Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane.The Journal of biological chemistry · 2025Article
- cAMP signaling ofmSphere · 2024Article
- Legionella maintains host cell ubiquitin homeostasis by effectors with unique catalytic mechanisms.Nature communications · 2024Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Legionella maintains host cell ubiquitin homeostasis by effectors with unique catalytic mechanisms.Research square · 2024Article
- Article
- CyaA translocation across eukaryotic cell membranes.Frontiers in molecular biosciences · 2024Article
- Discovery of a potent and selective human AC2 inhibitor based on 7-deazapurine analogues of adefovir.Bioorganic & medicinal chemistry · 2023Article
- Functional and structural insights into the multi-step activation and catalytic mechanism of bacterial ExoY nucleotidyl cyclase toxins bound to actin-profilin.PLoS pathogens · 2023Article
- Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium.BMC biology · 2022Article
- Article
- Bacterial Nucleotidyl Cyclases Activated by Calmodulin or Actin in Host Cells: Enzyme Specificities and Cytotoxicity Mechanisms Identified to Date.International journal of molecular sciences · 2022Review
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Review
- Halogen-Dance-Based Synthesis of Phosphonomethoxyethyl (PME) Substituted 2-Aminothiazoles as Potent Inhibitors of Bacterial Adenylate Cyclases.ChemMedChem · 2022Article
- Two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity.Frontiers in plant science · 2022Article
- A Bacterial Two-Hybrid System for In Vivo Assays of Protein-Protein Interactions and Drug Discovery.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Mechanism of actin-dependent activation of nucleotidyl cyclase toxins from bacterial human pathogens.Nature communications · 2021Article
- Structural and mechanistic basis for protein glutamylation by the kinase fold.Molecular cell · 2021Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
CyaA is crucial for colonization by Bordetella pertussis, the etiologic agent of whooping cough. Here we report crystal structures of the adenylyl cyclase domain (ACD) of CyaA with the C-terminal domain of calmodulin. Four discrete regions of CyaA bind calcium-loaded calmodulin with a large buried contact surface. Of those, a tryptophan residue (W242) at an alpha-helix of CyaA makes extensive contacts with the calcium-induced, hydrophobic pocket of calmodulin. Mutagenic analyses show that all four regions of CyaA contribute to calmodulin binding and the calmodulin-induced conformational change of CyaA is crucial for catalytic activation. A crystal structure of CyaA-calmodulin with adefovir diphosphate, the metabolite of an approved antiviral drug, reveals the location of catalytic site of CyaA and how adefovir diphosphate tightly binds CyaA. The ACD of CyaA shares a similar structure and mechanism of activation with anthrax edema factor (EF). However, the interactions of CyaA with calmodulin completely diverge from those of EF. This provides molecular details of how two structurally homologous bacterial toxins evolved divergently to bind calmodulin, an evolutionarily conserved calcium sensor.
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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.