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Showing 1–7 of 7 results
Advanced filters: Author: Rie Nygaard Clear advanced filters

  • Here the authors applied cryogenic time-resolved electron microscopy with rapid UV photolysis of a caged substrate to elucidate the catalytic mechanism of lipid-sugar transfer within the bacterial membrane by the glycosyltransferase GtrB.

    • Ryan T. Morgan
    • Stefano Motta
    • Filippo Mancia
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • Bacterial resistance to polymyxin antibiotics is conferred by enzymes such as phosphoethanolamine transferases, which add positively charged phosphoethanolamine to lipid A. Here, the authors present the structure of one such enzyme in its liganded form, and propose an enzymatic mechanism that may be generally applicable to other phosphoform transferases.

    • Allen P. Zinkle
    • Mariana Bunoro Batista
    • Filippo Mancia
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • Here, the authors present cryoEM structures of AftB, a key mycobacterial enzyme that adds terminal arabinose residues to the cell wall. In concert with functional assays and MD simulations, mechanistic insights are presented.

    • Yaqi Liu
    • Chelsea M. Brown
    • Filippo Mancia
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-16

  • Here the authors investigate of the structural basis of substrate recognition and the catalytic mechanism of the mannosyltransferase PimE, which is crucial for the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs) in Mycobacterium tuberculosis.

    • Yaqi Liu
    • Chelsea M. Brown
    • Filippo Mancia
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-17

  • Bacterial cell shape is dependent on the formation of the extracellular sugar polymer called peptidoglycan. Here the authors describe RodA-PBP2, the enzymatic core of the elongasome, which is the complex responsible peptidoglycan synthesis, and utilize an integrated approach to investigate the mechanism of peptidoglycan biosynthesis.

    • Rie Nygaard
    • Chris L. B. Graham
    • Filippo Mancia
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-15

  • Cryo-electron microscopy structures of the bacterial O-antigen ligase WaaL, combined with genetics, biochemistry and molecular dynamics simulations, provide insight into the mechanism by which WaaL catalyses the biosynthesis of lipopolysaccharide.

    • Khuram U. Ashraf
    • Rie Nygaard
    • Filippo Mancia
    Research
    Nature
    Volume: 604, P: 371-376

  • G-protein-coupled receptors (GPCRs) mediate the majority of cellular responses to hormones and neurotransmitters and are the largest group of therapeutic targets for a range of diseases. The extracellular surface (ECS) of GPCRs is diverse and therefore an ideal target for the discovery of subtype-selective drugs. Here, NMR spectroscopy is used to investigate ligand-specific conformational changes around a central structural feature in the ECS of a GPCR.

    • Michael P. Bokoch
    • Yaozhong Zou
    • Brian K. Kobilka
    Research
    Nature
    Volume: 463, P: 108-112