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Showing 1–10 of 10 results
Advanced filters: Author: Max J. Cryle Clear advanced filters

  • Antibiotic resistance in Staphylococcus aureus is associated with reduced neutrophil recruitment. Here, Payne et al. link formylated peptides, which act as chemoattractants for neutrophils, with the antibiotic vancomycin and show that these hybrid compounds improve clearance of S. aureus by neutrophils.

    • Jennifer A. E. Payne
    • Julien Tailhades
    • Max J. Cryle
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-15

  • Glycopeptide antibiotics (GPAs) are microbial natural products synthesized by multiple enzymes, including a nonribosomal peptide synthetase for assembly of the peptide core. Here, the authors use computational techniques to infer a gene set for biosynthesis of an ancestral GPA, produce the peptide in a microbial host, and provide insights into the evolution of key enzymatic domains.

    • Mathias H. Hansen
    • Martina Adamek
    • Nadine Ziemert
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-16

  • Kistamicin is a structurally divergent glycopeptide antibiotic (GPA) that contains a unique 15-membered A-O-B ring. Here, the authors obtained a crystal structure of the kistamicin OxyA/X-domain complex and analysed the cyclisation cascade leading to the formation of the A-O-B ring.

    • Anja Greule
    • Thierry Izoré
    • Max J. Cryle
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-15

  • Non-ribosomal peptide synthetases (NRPSs) are multi-modular enzymes assembling complex natural products. Here, the structures of a Thermobifida fusca NRPS condensation domain bound to the substrate-bearing peptidyl carrier protein (PCP) domain provide insight into the mechanisms of substrate selectivity and engagement within the catalytic pocket.

    • Thierry Izoré
    • Y. T. Candace Ho
    • Max J. Cryle
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14

  • A crucial malonic acid moiety in the antibiotic malonomycin has been shown to be installed by a bacterial vitamin K-dependent (VKD) carboxylase orthologue.

    • Max J. Cryle
    News & Views
    Nature Catalysis
    Volume: 1, P: 907-908

  • Glycopeptide antibiotics are biosynthesized by non-ribosomal peptide synthetases, which contain a previously uncharacterized ‘X-domain’ now shown to recruit three cytochrome P450 oxygenases that are necessary for the antibiotics to achieve their final, active conformation.

    • Kristina Haslinger
    • Madeleine Peschke
    • Max J. Cryle
    Research
    Nature
    Volume: 521, P: 105-109

  • X-ray crystallography and cryo-electron microscopy structures of the transcriptional repressor of the methylomycin gene cluster, MmfR, reveal the molecular basis for regulation of antibiotic biosynthesis by AHFCA hormones in Actinobacteria.

    • Shanshan Zhou
    • Hussain Bhukya
    • Christophe Corre
    Research
    Nature
    Volume: 590, P: 463-467

  • The repressor–antirepressor complex AppA–PpsR is a transcriptional regulator that permits Rhodobacter to switch between photosynthesis and respiration in response to light and oxygen. A combination of crystallography, hydrogen/deuterium-exchange MS and binding assays shows how illumination reduces the affinity of the complex for DNA and provides insight into the mechanism of signal transduction by photoreceptors.

    • Andreas Winkler
    • Udo Heintz
    • Ilme Schlichting
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 859-867

  • Hydrazine is an intermediate in the process of anaerobic ammonium oxidation which has a major role in the Earth’s nitrogen cycle; the crystal structure of a hydrazine synthase enzyme provides insights into the mechanism of hydrazine synthesis.

    • Andreas Dietl
    • Christina Ferousi
    • Thomas R. M. Barends
    Research
    Nature
    Volume: 527, P: 394-397