Blar i forfatter "Røhr, Åsmund Kjendseth"

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    • The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection 

      Askarian, Fatemeh; Uchiyama, Satoshi; Masson, Helen; Sørensen, Henrik Vinther; Golten, Ole; Bunæs, Anne Cathrine; Mekasha, Sophanit; Røhr, Åsmund Kjendseth; Kommedal, Eirik Garpestad; Ludviksen, Judith Anita; Arntzen, Magnus Øverlie; Schmidt, Benjamin; Zurich, Raymond H.; Van Sorge, Nina M.; Eijsink, Vincent; Krengel, Ute; Mollnes, Tom Eirik; Lewis, Nathan E.; Nizet, Victor; Vaaje-Kolstad, Gustav (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-02-23)
      The recently discovered lytic polysaccharide monooxygenases (LPMOs), which cleave polysaccharides by oxidation, have been associated with bacterial virulence, but supporting functional data is scarce. Here we show that CbpD, the LPMO of <i>Pseudomonas aeruginosa</i>, is a chitin-oxidizing virulence factor that promotes survival of the bacterium in human blood. The catalytic activity of CbpD was ...

    • The Methylococcus capsulatus (Bath) secreted protein, MopE*, binds both reduced and oxidized copper. 

      Ve, Thomas; Mathisen, Karina; Helland, Ronny; Karlsen, Odd Andre; Fjellbirkeland, Anne; Røhr, Åsmund Kjendseth; Andersson, K. Kristoffer; Pedersen, Rolf B.; Lillehaug, Johan R.; Jensen, Harald B (Journal article; Tidsskriftartikkel; Peer reviewed, 2012)
      Under copper limiting growth conditions the methanotrophic bacterium Methylococcus capsulatus (Bath) secrets essentially only one protein, MopE*, to the medium. MopE* is a copper-binding protein whose structure has been determined by X-ray crystallography. The structure of MopE* revealed a unique high affinity copper binding site consisting of two histidine imidazoles and one kynurenine, the latter ...