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Figure 2.
Figure 2. Structure of the P4 Hexamer(A) The P4 hexamer is
shown in terms of its secondary structural elements and solvent
accessible surface in top, side, and bottom views. The secondary
structural elements are colored according to the bar where
different colors distinguish subdomains or segments of the P4
monomer: N-terminal safety pin motif (blue), all β domain (dark
purple), conserved RecA-like ATP binding domain (red), and
antiparallel β strands and C-terminal helix (green). Six
molecules of AMPcPP, drawn as ball-and-stick representations,
are located in clefts between monomers. The solvent-accessible
surface of P4 (without nucleotides) is colored according to the
electrostatic potential (defined in the key). The top view shows
the solvent-exposed face of the P4 hexamer, while the bottom
view shows the C-terminal face that packs against the procapsid.
Representations and calculations were performed with GRASP
(Nicholls et al., 1991).(B) Cartoon showing the position of the
P4 hexamer (red) on the empty φ12 procapsid (green) while
packaging ssRNA (cyan).
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