Neumann, Piotr D.Piotr D.NeumannHeidemann, Jana L.Jana L.HeidemannWollenhaupt, JanJanWollenhauptDickmanns, AchimAchimDickmannsAgthe, MichaelMichaelAgtheWeiss, Manfred S.Manfred S.WeissFicner, RalfRalfFicner2024-05-202024-05-202024https://resolver.sub.uni-goettingen.de/purl?gro-2/143177CdaA 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.https://creativecommons.org/licenses/by/4.0/legalcodejournal_article10.1107/S205979832400336XS205979832400336X