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. 2009 Jul 22;284(38):26174–26183. doi: 10.1074/jbc.M109.021907

FIGURE 1.

FIGURE 1.

A, ribbon diagram of unliganded MvNei1. The model from form II crystals comprises residues 2–289. The secondary structure elements were defined by DSSP (59) and are as follows: αA (4–18), β1 (22–27), αB (41–45), β2 (50–58), β3 (61–67), β4 (75–81), β5 (87–89), β6 (96–102), β7 (107–111), β8 (118–122), αC (125–133), αD (157–162), αE (173–183), αF (196–215), αG (226–229), β9 (265–267), and β10 (279–281). Helices are shown in light green and β-strands in magenta. The putative lesion binding loop is highlighted in a darker shade of green. B, comparison of MvNei1 with E. coli Nei (EcoNei). Superposition of MvNei1 (pink) with unliganded EcoNei (gray; PDB code 1Q3B (30) and the EcoNei trapped DNA complex (black; PDB code 1K3W (23)). C, close-up of the zinc-finger motif. Shown are residues 230–262 for EcoNei, 263–290 for hNEIL1, and 253–289 for MvNei1. The asterisks indicate the position of the Cα of the conserved arginine (Arg-252 in EcoNei and Arg-277 in hNEIL1 and MvNei1).

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