Selected article for: "Î helix and Î strand"
Author: Dene Littler; Benjamin Gully; Rhys N Colson; Jamie Rossjohn
Title: Crystal structure of the SARS-CoV-2 non-structural protein 9, Nsp9
  • Document date: 2020_3_30
    • ID: beoseizn_9
    Snippet: We next determined the structure of apo-Nsp9COV19 (Table 1 ). The apo-Nsp9COV19 structure aligned closely to that of Nsp9SARS (R.M.S.D of 0.57Å over 113 Cα, Fig. 2A -C) (Egloff et al., 2004) . Like other Nsp9 homologues it exhibits an unusual fold that is yet to be observed outside of coronaviruses (Sutton et al., 2004) . The core of the fold is a small 6-stranded enclosed β-barrel, from which a series of extended loops project outward (Fig 2A.....
    Document: We next determined the structure of apo-Nsp9COV19 (Table 1 ). The apo-Nsp9COV19 structure aligned closely to that of Nsp9SARS (R.M.S.D of 0.57Å over 113 Cα, Fig. 2A -C) (Egloff et al., 2004) . Like other Nsp9 homologues it exhibits an unusual fold that is yet to be observed outside of coronaviruses (Sutton et al., 2004) . The core of the fold is a small 6-stranded enclosed β-barrel, from which a series of extended loops project outward (Fig 2A) . The elongated loops link the individual β-strands of the barrel, along with a projecting N-terminal βstrand and C-terminal α1-helix; the latter two elements make up the main Fluorescence polarization anisotropy assays were used to examine the possibility that Nsp9COV19 could bind to labelled 17-mer and 10-mer single stranded oligonucleotides. The plot shows corrected anisotropy for each Nsp9COV19 protein concentration, error bars represent the SD from the mean of triplicate measurements after 60 minutes incubation.

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