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17 reviewsC5-glyceryl-methylcytosine (5gmC) is a novel DNA modification catalyzed by algal TEThomologue CMD1 using vitamin C (VC) as co-substrate. Here, we report the structures ofCMD1 in apo form and in complexes with VC or/and dsDNA. CMD1 exhibits comparablebinding affinities for DNAs of different lengths, structures, and 5mC levels, and displays amoderate substrate preference for 5mCpG-containing DNA. CMD1 adopts the typical DSBHfold of Fe2+/2-OG-dependent dioxygenases. The lactone form of VC binds to the active siteand mono-coordinates the Fe2+ in a manner different from 2-OG. The dsDNA binds to apositively charged cleft of CMD1 and the 5mC/C is inserted into the active site and recognized by CMD1 in a similar manner as the TET proteins. The functions of key residues arevalidated by mutagenesis and activity assay. Our structural and biochemical data togetherreveal the molecular mechanism for the VC-derived 5gmC DNA modification by CMD1.
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