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A small step towards an important goal: fragment screen of the c-di-AMP-synthesizing enzyme CdaA.
Neumann, Piotr; Heidemann, Jana L; Wollenhaupt, Jan; Dickmanns, Achim; Agthe, Michael; Weiss, Manfred S; Ficner, Ralf.
Afiliación
  • Neumann P; Department of Molecular Structural Biology, Institute of Microbiology and Genetics, GZMB, Georg-August-University Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.
  • Heidemann JL; Department of Molecular Structural Biology, Institute of Microbiology and Genetics, GZMB, Georg-August-University Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.
  • Wollenhaupt J; Macromolecular Crystallography, Helmholtz-Zentrum Berlin, Albert-Einstein-Strasse 15, 12489 Berlin, Germany.
  • Dickmanns A; Department of Molecular Structural Biology, Institute of Microbiology and Genetics, GZMB, Georg-August-University Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.
  • Agthe M; Institut für Nanostruktur- und Festkörperphysik, Universität Hamburg, Luruper Chaussee 149, 22761 Hamburg, Germany.
  • Weiss MS; Macromolecular Crystallography, Helmholtz-Zentrum Berlin, Albert-Einstein-Strasse 15, 12489 Berlin, Germany.
  • Ficner R; Department of Molecular Structural Biology, Institute of Microbiology and Genetics, GZMB, Georg-August-University Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.
Acta Crystallogr D Struct Biol ; 80(Pt 5): 350-361, 2024 May 01.
Article en En | MEDLINE | ID: mdl-38682668
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Listeria monocytogenes Límite: Humans Idioma: En Revista: Acta Crystallogr D Struct Biol Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Listeria monocytogenes Límite: Humans Idioma: En Revista: Acta Crystallogr D Struct Biol Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos