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. 2021 Nov 26;12:6942. doi: 10.1038/s41467-021-27284-7

Fig. 6. Molecular basis of C10R5 substrate specificity.

Fig. 6

a, b Close-up views of YtkR2 (a) and C10R5 (b) homology models bound to AP-DNA and YTM-Ade. Hydrogen-bonding interactions are indicated with dashed lines. c Truncated sequence alignment of AlkD, YtkR2, and C10R5. Residues that interact with AP-DNA and YTM-Ade in the AlkD product complex (PDB accession 5UUG) are indicated with orange triangles and magenta circles, respectively. d Single-turnover excision of YTM-Ade by wild-type and mutant C10R5. Reactions contained 1 μM enzyme and 100 nM DNA. e Multiple-turnover excision of YTM-Ade by wild-type and mutant C10R5. Reactions contained 10 nM enzyme and 100 nM DNA. Mutated residues are indicated with bold font in a and b and with black circles in c. Data in d and e are presented as the mean ± SD from three replicate experiments. Source data are provided as a Source Data file. f YTM resistance conferred by C10R5 mutants. E. coli BL21(DE3) cells were transformed with either an empty plasmid (blank) or a plasmid encoding YtkR2, C10R5, or one of two C10R5 mutants, and grown in the absence or presence of YTM. Experiments were performed in duplicate.