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Articles by Rie Nygaard
Mechanistic snapshots of lipid-linked sugar transfer - Nature Communications
Abstract Enzymes undergo dynamic conformational changes during catalysis, yet conventional high-resolution structural methods typically capture only the most stable states. Here, we address this gap using rapid UV photolysis of a chemically caged substrate with cryogenic time-resolved electron microscopy (cryo-TREM). We elucidate the catalytic mechanism of GtrB, a membrane-bound glycosyltransferase that transfers glucose from UDP-glucose to the lipid carrier undecaprenyl phosphate.
Mechanistic basis of antimicrobial resistance mediated by the phosphoethanolamine transferase MCR-1 - Nature Communications
Abstract Polymyxins are used to treat infections caused by multidrug-resistant Gram-negative bacteria. They are cationic peptides that target the negatively charged lipid A component of lipopolysaccharides, disrupting the outer membrane and lysing the cell. Polymyxin resistance is conferred by inner-membrane enzymes, such as phosphoethanolamine transferases, which add positively charged phosphoethanolamine to lipid A.
Mechanistic studies of mycobacterial glycolipid biosynthesis by the mannosyltransferase PimE - Nature Communications
Abstract Tuberculosis (TB), a leading cause of death among infectious diseases globally, is caused by Mycobacterium tuberculosis (Mtb). The pathogenicity of Mtb is largely attributed to its complex cell envelope, which includes a class of glycolipids called phosphatidyl-myo-inositol mannosides (PIMs). These glycolipids maintain the integrity of the cell envelope, regulate permeability, and mediate host-pathogen interactions.
Lipid Research Division
About the LRD The Lipid Research Division is a division of the American Society for Biochemistry and Molecular Biology. The LRD represents lipid research scientists of the society and addresses concerns that include, but are not limited to, national and international visibility, representation at the annual meeting and on scientific advisory panels, and increased funding for lipid research.
Structural Basis of WLS/Evi-Mediated Wnt Transport and Secretion
Highlights • We present the cryo-EM structure of human WNT8A in complex with its transporter WLS • The WLS membrane domain has structural homology to GPCRs • WLS harbors the Wnt palmitoleate in a hydrophobic cavity in its membrane domain • A conformational switch on Wnt hairpin 3 might favor unidirectional Wnt transfer Summary Wnts are evolutionarily conserved ligands that signal at short range to regulate morphogenesis, cell fate, and stem cell renewal.
Structural Basis of WLS/Evi-Mediated Wnt Transport and Secretion
Adams P.D. Afonine P.V. Bunkóczi G. Chen V.B. Davis I.W. Echols N. Headd J.J. Hung L.-W. Kapral G.J. Grosse-Kunstleve R.W. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 2010; 66: 213-221 Afonine P.V. Poon B.K. Read R.J. Sobolev O.V. Terwilliger T.C. Urzhumtsev A. Adams P.D. Real-space refinement in PHENIX for cryo-EM and crystallography. Acta Crystallogr. D Struct. Biol.
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