Figure 8.
Figure 8 Models for dsDNA interacting with drRecO based on the
DNA-binding studies and mutational analysis. In (A), the
secondary structure succession is outlined in colours ranging
from blue to red. Some positively charged residues are shown for
comparison to positive regions seen in the estimated
electrostatic surface potentials. Residues mutated in this study
are labelled in red. The electrostatic surface potentials in (B
-E) are contoured at 3
kT/e, where red describes a negative and blue a positive
potential. dsDNA interacting with drRecO is modelled as sticks
in (B, C). Two alternative binding sites involving the OB barrel
(bottom) and a positive patch (190-RHAVRRTVR-200) unique for
drRecO ending at the zinc-finger (top) are shown. (D) Close-up
of dsDNA modelled to interact with the positive patch unique to
drRecO with positively charged residues labelled. (E) Close-up
of the region in the OB barrel found to be important for dsDNA
binding in drRecO. (F) Indication of how well the mutants of
drRecO bind to DNA; +++, unaffected DNA-binding ability; +,
reduced DNA-binding ability; -, loss of DNA-binding ability.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2005,
24,
906-918)
copyright 2005.
3
kT/e, where red describes a negative and blue a positive
potential. dsDNA interacting with drRecO is modelled as sticks
in (B, C). Two alternative binding sites involving the OB barrel
(bottom) and a positive patch (190-RHAVRRTVR-200) unique for
drRecO ending at the zinc-finger (top) are shown. (D) Close-up
of dsDNA modelled to interact with the positive patch unique to
drRecO with positively charged residues labelled. (E) Close-up
of the region in the OB barrel found to be important for dsDNA
binding in drRecO. (F) Indication of how well the mutants of
drRecO bind to DNA; +++, unaffected DNA-binding ability; +,
reduced DNA-binding ability; -, loss of DNA-binding ability.