ArticleJournal of molecular biology2012
Crystal structure and regulation mechanisms of the CyaB adenylyl cyclase from the human pathogen Pseudomonas aeruginosa.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 44 citations in OpenAlex.
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- The Catabolite Repression Control Protein Crc Regulates the Type III Secretion System Through the Adenylate Cyclase CyaB inMicroorganisms · 2025Article
- Twitching motility suppressors reveal a role for FimX in type IV pilus extension dynamics.PLoS genetics · 2025Article
- Antagonistic response regulators spatially regulate receptor methylation in the Pseudomonas aeruginosa Pil-Chp surface sensing system.Cell reports · 2025Article
- A bacterial sense of touch: T4P retraction motor as a means of surface sensing byJournal of bacteriology · 2024Review
- Unraveling the molecular dynamics ofFuture microbiology · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
- How Bacterial Pathogens Coordinate Appetite with Virulence.Microbiology and molecular biology reviews : MMBR · 2023Review
- The virulence factor regulator and quorum sensing regulate the type I-F CRISPR-Cas mediated horizontal gene transfer inFrontiers in microbiology · 2022Article
- Bicarbonate Evokes Reciprocal Changes in Intracellular Cyclic di-GMP and Cyclic AMP Levels inBiology · 2021Article
- How Do Shipworms Eat Wood? Screening Shipworm Gill Symbiont Genomes for Lignin-Modifying Enzymes.Frontiers in microbiology · 2021Article
- The diguanylate cyclase AdrA regulates flagellar biosynthesis in Pseudomonas fluorescens F113 through SadB.Scientific reports · 2019Article
- NrtR Regulates the Type III Secretion System Through cAMP/Vfr Pathway inFrontiers in microbiology · 2019Article
- Pharmacological modulation of the COPharmacology & therapeutics · 2018Review
- Role of the nucleotidyl cyclase helical domain in catalytically active dimer formation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Cyclic AMP-Independent Control of Twitching Motility in Pseudomonas aeruginosa.Journal of bacteriology · 2017Article
- Phosphoryl Group Flow within the Pseudomonas aeruginosa Pil-Chp Chemosensory System: DIFFERENTIAL FUNCTION OF THE EIGHT PHOSPHOTRANSFERASE AND THREE RECEIVER DOMAINS.The Journal of biological chemistry · 2016Article
- The Conserved Tetratricopeptide Repeat-Containing C-Terminal Domain of Pseudomonas aeruginosa FimV Is Required for Its Cyclic AMP-Dependent and -Independent Functions.Journal of bacteriology · 2016Article
- Twitching motility and cAMP levels: signal transduction through a single methyl-accepting chemotaxis protein.FEMS microbiology letters · 2016Article
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
Pseudomonas aeruginosa is an opportunistic bacterial pathogen and a major cause of healthcare-associated infections. While the organism's intrinsic and acquired resistance to most antibiotics hinders treatment of P. aeruginosa infections, the regulatory networks controlling its virulence provide novel targets for drug development. CyaB, a key regulator of P. aeruginosa virulence, belongs to the Class III adenylyl cyclase (AC) family of enzymes that synthesize the second messenger cyclic adenosine 3',5'-monophosphate. These enzymes consist of a conserved catalytic domain fused to one or more regulatory domains. We describe here the biochemical and structural characterization of CyaB and its inhibition by small molecules. We show that CyaB belongs to the Class IIIb subfamily, and like other subfamily members, its activity is stimulated by inorganic carbon. CyaB is also regulated by its N-terminal MASE2 (membrane-associated sensor 2) domain, which acts as a membrane anchor. Using a genetic screen, we identified activating mutations in CyaB. By solving the crystal structure of the CyaB catalytic domain, we rationalized the effects of these mutations and propose that CyaB employs regulatory mechanisms similar to other Class III ACs. The CyaB structure further indicates subtle differences compared to other Class III ACs in both the active site and the inhibitor binding pocket. Consistent with these differences, we observed a unique inhibition profile, including identification of a CyaB selective compound. Overall, our results reveal mechanistic details of the physiological and pharmacological regulation of CyaB and provide the basis for its exploitation as a therapeutic drug target.
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