Crystal structure of a class III adenylyl cyclase-like ATP-binding protein from Pseudomonas aeruginosa

Linder, Juergen U.; Hupfeld, Enrico; Weyand, Michael; Steegborn, Clemens; Moniot, S.

doi:10.1016/j.jsb.2020.107534

Cited by 5 publications

(1 citation statement)

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“…These ranged from their lower availability in the cell compared with, for example, ATP, to their limited capacity for hydrogen bonding and base stacking interactions compared with their purine‐containing counterparts. This dogma is further highlighted by the crystal structure of the uridylate cyclase PycC from Pseudomonas aeruginosa , which was initially assumed to use ATP as a substrate due to high structural homology with mammalian type III adenylate cyclases [54]. However, most recently PycC, a member of the Pycsar anti‐phage defense system, was confirmed to catalytically produce cUMP from UTP [47].…”

Section: Milestones In Cyclic Nucleotide Researchmentioning

confidence: 99%

How enzyme‐centered approaches are advancing research on cyclic oligo‐nucleotides

Wenzl,

de Oliveira Mann

2024

FEBS Letters

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Cyclic nucleotides are the most diversified category of second messengers and are found in all organisms modulating diverse pathways. While cAMP and cGMP have been studied over 50 years, cyclic di‐nucleotide signaling in eukaryotes emerged only recently with the anti‐viral molecule 2´3´cGAMP. Recent breakthrough discoveries have revealed not only the astonishing chemical diversity of cyclic nucleotides but also surprisingly deep‐rooted evolutionary origins of cyclic oligo‐nucleotide signaling pathways and structural conservation of the proteins involved in their synthesis and signaling. Here we discuss how enzyme‐centered approaches have paved the way for the identification of several cyclic nucleotide signals, focusing on the advantages and challenges associated with deciphering the activation mechanisms of such enzymes.

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Section: Milestones In Cyclic Nucleotide Researchmentioning

confidence: 99%