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A small step towards an important goal: fragment screen of the c-di-AMP-synthesizing enzyme CdaA.
- Source :
-
Acta crystallographica. Section D, Structural biology [Acta Crystallogr D Struct Biol] 2024 May 01; Vol. 80 (Pt 5), pp. 350-361. Date of Electronic Publication: 2024 Apr 29. - Publication Year :
- 2024
-
Abstract
- CdaA is the most widespread diadenylate cyclase in many bacterial species, including several multidrug-resistant human pathogens. The enzymatic product of CdaA, cyclic di-AMP, is a secondary messenger that is essential for the viability of many bacteria. Its absence in humans makes CdaA a very promising and attractive target for the development of new antibiotics. Here, the structural results are presented of a crystallographic fragment screen against CdaA from Listeria monocytogenes, a saprophytic Gram-positive bacterium and an opportunistic food-borne pathogen that can cause listeriosis in humans and animals. Two of the eight fragment molecules reported here were localized in the highly conserved ATP-binding site. These fragments could serve as potential starting points for the development of antibiotics against several CdaA-dependent bacterial species.<br /> (open access.)
- Subjects :
- Crystallography, X-Ray methods
Binding Sites
Bacterial Proteins chemistry
Bacterial Proteins metabolism
Models, Molecular
Dinucleoside Phosphates metabolism
Dinucleoside Phosphates chemistry
Anti-Bacterial Agents pharmacology
Humans
Phosphorus-Oxygen Lyases chemistry
Phosphorus-Oxygen Lyases metabolism
Protein Conformation
Listeria monocytogenes enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 2059-7983
- Volume :
- 80
- Issue :
- Pt 5
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section D, Structural biology
- Publication Type :
- Academic Journal
- Accession number :
- 38682668
- Full Text :
- https://doi.org/10.1107/S205979832400336X