Figure 6.
The residues of DBD-A and DBD-B implicated in Tag-protein interactions and the evolutionarily conserved residues that may be involved in interactions with cellular factors map to overlapping surfaces. (A) Molecular surface of the Rpa–oligo(dT)32 complex in an orientation related to that of Figure 1A by an ∼180° rotation about the vertical axis. The individual Rpa subunits are colored as in Figure 1B, and their domains are labeled. DNA is in blue. The U. maydis Rpa residues corresponding to the human RPA DBD-A–DBD-B residues implicated in SV40 Tag binding are colored in red and labeled according to the alignment in Supplemental Figure S3. (B) Molecular surface of the Rpa–oligo(dT)32 complex, colored according to sequence conservation in the U. maydis, human, zebrafish, fly, budding yeast, and fission yeast Rpa, with red indicating identity in all orthologs. The left panel view is as in A, and the right panel view is as in Figure 1B.