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Figure 3.
Figure 3 Study of the ionic interactions between drRecO and
drRecR. (A) Ribbon illustration of a monomer and a tetramer of
drRecR with ball-and-sticks representation of the mutated
residues. (B) Ribbon illustration of drRecO with ball-and-sticks
representation of the mutated residues. Residues coloured in
blue were mutated in order to disrupt protein–protein
interactions, whereas residues in red were predicted to be
involved in protein–DNA contacts. (C) Overlay of the
chromatograms obtained when purifying wild-type drRecOR (C1) and
mutant drRecOR (C2) on a Superdex 200 size-exclusion column. The
three peaks are labelled from 1 to 3. (D) Western blot analysis
of fractions corresponding to peaks 1, 2 and 3 from the gel
filtration runs of each of the drRecOR complexes (C1–C7 and
C10–C16). The Western blots were duplicated and were stained
for either drRecO (upper bands) or drRecR (lower bands). (E)
Illustration of the drRecR (gold)—drRecO (blue) interface with
a ball-and-sticks representation of drRecO-His93 and
drRecR-Glu146, displaying the 2mFo-DFc sigmaA-weighted electron
density map contoured at 1.3  .
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