Figure_2.tif (1.98 MB)

Structure of the SUDcore monomer and comparison with the SARS-CoV X-domain.

Download (0 kB)
figure
posted on 15.05.2009, 02:37 by Jinzhi Tan, Clemens Vonrhein, Oliver S. Smart, Gerard Bricogne, Michela Bollati, Yuri Kusov, Guido Hansen, Jeroen R. Mesters, Christian L. Schmidt, Rolf Hilgenfeld

(A) Ribbon representation of the SUDcore structure (residues 389–652 of Nsp3). The flexible linker connecting the two macrodomains is indicated by a dotted line. The disulfide bond between cysteines 492 of SUD-N and 623 of SUD-M is shown in orange. (B) Stereo image of the 2Fo–Fc electron-density map (1σ above the mean) around the disulfide bond connecting the SUD-N and SUD-M subdomains. (C) Structure-based sequence alignment of the SUDcore subdomains N (SUD-N) and M (SUD-M), and the SARS-CoV X-domain (SARS-X). α-Helices and β-strands are marked red and blue, respectively. Residues 518–524 form the linker between the two SUD subdomains and have not been included in the alignment. Asterisks mark SARS-X residues involved in binding of ADP-ribose. (D) Superimposition of the structures of the SUD-N (violet) and SUD-M (green) subdomains with the SARS-CoV X-domain (cyan).

History

Licence

Exports

Logo branding

Licence

Exports