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. 2006 Dec 6;35(1):87–99. doi: 10.1093/nar/gkl1010

Figure 6.

Figure 6

The Pcf11 binding site. (a) A surface representation of Clp1, The domains are coloured as in Figure 2, Pcf11 is shown as a cartoon representation and the highly conserved residues R480, W482 and W489 that make interactions with Clp1 are shown in the stick representation. (b) A schematic diagram displaying the protein–protein contacts observed at the Clp1–Pcf11 interface. Pcf11 residues are represented with ellipses, Clp1 residues by rectangles. The residues in Pcf11 that make contacts with Clp1 are highlighted in blue, hydrogen bonding interactions are shown as black dashed lines and hydrophobic interactions in green. (c) Details of the conserved arginine 480 interactions. R480 and the residues from the Clp1 central domain that are involved in hydrogen bonding interactions are shown in stick representation. The domains are coloured as in Figure 2. (d) A sequence alignment of the Clp1-binding region from Pcf11. The residues identical to the S.cerevisiae sequence are boxed and the residues that are conserved in all organisms are coloured red.