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Figure 1.
FIGURE 1. Structure of SARS-CoV Nsp15. A, surface
representation of a subunit showing three domains. Active site
residues are colored by element and indicated by an arrow. B,
arrangement of six subunits from top view of hexamer.
N-terminal, middle, and C-terminal domains are indicated as N,
M, and C, respectively. The arrows indicate the positions of
catalytic sites in top trimer. C, side view of hexamer showing
arrangement and N- to N-terminal interaction of the top trimer
(T1) with bottom trimer (T2). Six subunits are labeled as a-c
and are colored as follows: T1a, pink; T1b, blue; T1c, cyan;
T2a, red; T2b, green; T2c, golden. This color scheme is used
throughout the figures. Catalytic residues are colored yellow.
D, worm diagram drawn based on b-factor. Worm thickness is
directly proportional to flexibility, i.e. the thickest region
indicates most flexible. E, overlap of the catalytic residues
within the active sites of the six subunits. The structures are
anchored by the backbond of His^249.
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