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Showing 1–13 of 13 results
Advanced filters: Author: Peter J. Stogios Clear advanced filters

  • Antibiotic resistance is a major clinical problem that threatens to undermine our ability to control infectious diseases. Here the authors present detailed structural analysis of Rifampin phosphotransferase from Listeria monocytogenes, yielding insight on how this class of enzyme inactivates its target antibiotics.

    • Peter J. Stogios
    • Georgina Cox
    • Gerard D. Wright
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-12

  • Bacterial resistance to sulfonamide antibiotics (sulfas) is mediated by acquisition of sul genes, which encode sulfa-insensitive versions of the target enzyme, dihydropteroate synthase. Here, Venkatesan et al. study Sul enzymes using biochemical, structural, mutational and functional analyses, revealing the molecular basis for Sul-mediated drug resistance.

    • Meenakshi Venkatesan
    • Michael Fruci
    • Alexei Savchenko
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-17

  • Strigolactone (SL) regulates plant development. Structural analysis shows that when SL binds its receptor ShHTL5, conformational changes occur including the creation of internal tunnels that posit an explanation for how SL by-products exit the receptor after signalling.

    • Amir Arellano-Saab
    • Tatiana Skarina
    • Peter McCourt
    Research
    Nature Plants
    Volume: 9, P: 883-888

  • Here, the authors describe the mechanistic flexibility and substrate promiscuity of the apramycin resistance enzyme ApmA. They identify additional clinical drugs susceptible to modification through a molecular mechanism that diverges from other enzymes within the left-handed β-helix superfamily.

    • Emily Bordeleau
    • Peter J. Stogios
    • Gerard D. Wright
    Research
    Nature Chemical Biology
    Volume: 20, P: 234-242

  • Oleispira antarctica is an oil-degrading bacterium found in the cold and deep sea. Here Kube et al. report the genome sequence of O. antarcticaand provide a comprehensive functional genetic and protein structural analysis, revealing insights into how this organism has adapted to its cold environment.

    • Michael Kube
    • Tatyana N. Chernikova
    • Peter N. Golyshin
    ResearchOpen Access
    Nature Communications
    Volume: 4, P: 1-11

  • Alterations of the mucosal microbiota, including Lactobacillus bacteria, are associated with infections caused by the fungus Candida albicans. Here, MacAlpine et al. show that some Lactobacillus strains produce a small molecule that blocks C. albicans filamentation and biofilm formation, and thus virulence, through inhibition of a fungal kinase.

    • Jessie MacAlpine
    • Martin Daniel-Ivad
    • Leah E. Cowen
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-16

  • The bacterium Pseudomonas aeruginosa attacks competing bacteria using the toxin Tas1, which pyrophosphorylates adenosine nucleotides to generate (p)ppApp, thereby depleting ATP and disrupting multiple cellular functions.

    • Shehryar Ahmad
    • Boyuan Wang
    • John C. Whitney
    Research
    Nature
    Volume: 575, P: 674-678

  • SH2 domains bind to tyrosine-phosphorylated proteins and play crucial roles in signal transduction in mammalian cells. Here, Kaneko et al. identify a large family of SH2 domains in the bacterial pathogen Legionella that bind to mammalian phosphorylated proteins, in some cases with very high affinity.

    • Tomonori Kaneko
    • Peter J. Stogios
    • Shawn S.-C. Li
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-15

  • New antibiotics with reduced potential for resistance are urgently needed. Here, the authors use a multidisciplinary approach to characterize substrate discrimination in macrolide resistance kinases and present a strategy for the prediction of mutations that expand the substrate range of antibiotic-inactivating enzymes.

    • Andrew C. Pawlowski
    • Peter J. Stogios
    • Gerard D. Wright
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-12