|
Figure 6.
FIG. 6. Model of residues 192-319 of NEIL2. A, structural
alignment for NEIL2 and E. coli Fpg (PDB code 1K82 [PDB]
) template generated by 3DPSSM. Identical residues are indicated
by asterisks. Residues that participate in coordination of zinc
ion are highlighted in red and boldface. B, ribbon diagram of a
model of C-terminal region of NEIL2 generated using MOLMOL (49).
The helices (shown in green) form the helix two-turn helix motif
that binds to DNA. CHCC-type  -hairpin zinc finger is
highlighted with coordinating residues Cys-291, His-295,
Cys-315, and Cys-318. C, ribbon diagram of model of C-terminal
region of NEIL2 with DNA generated with MOLMOL. The helices
(shown in blue) form the helix two-turn helix motif that binds
to DNA. CHCC-type -hairpin zinc finger is
highlighted with coordinating residues Cys-291, His-295,
Cys-315, and Cys-318. The zinc ion stabilizes -strands
(shown in green) that is critical to position of the catalytic
residue Arg-310, which is conserved in E. coli Fpg.
|
