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Figure 2.
FIG. 2. The hexamer model of Hp ClpX-ASD and E. coli ClpP
heptamer. The ribbon diagrams of the hexamer model of Hp
ClpX-ASD viewed along the 6-fold axis from the protease
interface (A) and from the side (B) are shown. The same color
schemes as described in the legend to Fig. 1A are used. However,
each subunit is colored with a different brightness. The N and C
termini of one subunit are labeled. The surface charge
distribution of Hp ClpX-ASD (C) and E. coli ClpP (D) is shown.
The protease interface of Hp ClpX and the ATPase interface of
ClpP are drawn to show the possible ClpX-ClpP interface. The red
and blue areas represent the negatively and positively charged
surfaces, respectively. The white region represents the
hydrophobic surface. The LGF peptide of ClpX (residues 297, 298,
and 299), and the conserved hydrophobic cleft of ClpP (residues
60, 62, 82, 90, 92, 112, 114, and 189), are colored in yellow.
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