Blar i forfatter "Leiros, Hanna-Kirsti Schrøder"

Viser treff 1-4 av 4

    • Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase 

      Pan, Jolyn; Lian, Kjersti; Sarre, Aili; Leiros, Hanna-Kirsti Schrøder; Williamson, Adele Kim (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-09-21)
      DNA ligases, the enzymes responsible for joining breaks in the phosphodiester backbone of DNA during replication and repair, vary considerably in size and structure. The smallest members of this enzyme class carry out their functions with pared-down protein scaffolds comprising only the core catalytic domains. Here we use sequence similarity network analysis of minimal DNA ligases from all biological ...

    • Biochemical and biophysical characterization of the OXA-48-like carbapenemase OXA-436 

      Lund, Bjarte Aarmo; Thomassen, Ane Molden; Carlsen, Trine Josefine Warg; Leiros, Hanna-Kirsti Schrøder (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-08-31)
      The crystal structure of the class D β-lactamase OXA-436 was solved to a resolution of 1.80 Å. Higher catalytic rates were found at higher temperatures for the clinically important antibiotic imipenem, indicating better adaptation of OXA-436 to its mesophilic host than OXA-48, which is believed to originate from an environmental source. Furthermore, based on the most populated conformations during ...

    • Side-Chain Interactions in d/l Peptide Nanotubes: Studies by Crystallography, NMR Spectroscopy and Molecular Dynamics 

      Silk, Mitchell Ramesh; Price, Jason R.; Mohanty, Biswaranjan; Leiros, Hanna-Kirsti Schrøder; Lund, Bjarte Aarmo; Thompson, Phillip E.; Chalmers, David (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-08-20)
      Our understanding of the factors affecting the stability of cyclic d / l peptide (CP) nanotubes remains underdeveloped. In this work, we investigate the impact of side chain alignment, hydrophobicity and charge on CP nanotube stability through X-ray crystallography, NMR spectroscopy and molecular dynamics (MD) simulations. We characterise the distinct CP-CP alignments that can form and identify ...

    • Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1 

      Frøhlich, Christopher; Sørum, Vidar; Huber, Sandra; Samuelsen, Ørjan; Berglund, Fanny; Kristiansson, Erik; Kotsakis, Stathis D.; Marathe, Nachiket; Larsson, DG Joakim; Leiros, Hanna-Kirsti Schrøder (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-05-28)
      Background: MBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to b-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure–activity relationships ...