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_28
Snippet: Our preliminary nucleotide binding assays brought into question the RNA binding capacity of Nsp9COV19. The structure of the Nsp9COV19 showed conservation of the unique Nsp9 fold when compared with homologues from SARS (Egloff et al., 2004) (Sutton et al., 2004) . Indeed, the topological fold was conserved as was the Nsp9 specific ahelical GxxxG dimerisation interface. This a-helical interface is encircled by hydrophobic residues but the interface.....
Document: Our preliminary nucleotide binding assays brought into question the RNA binding capacity of Nsp9COV19. The structure of the Nsp9COV19 showed conservation of the unique Nsp9 fold when compared with homologues from SARS (Egloff et al., 2004) (Sutton et al., 2004) . Indeed, the topological fold was conserved as was the Nsp9 specific ahelical GxxxG dimerisation interface. This a-helical interface is encircled by hydrophobic residues but the interface includes considerable cavities as observed previously (Egloff et al., 2004) . We made a serendipitous discovery in our 3C-Nsp9COV19 structure, whereby the hydrophobic cavity captured the 3C cleavage sequence LEVL. The extraneous residues were tightly bound on all sides within the site situating themselves proximal to the conserved GxxxG motif. Coordination of the 3C sequence induced changes within interfacing residues, serving to both restructure key structural elements and cause a modest shift in subunit orientation.
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