Fig. 4: Structural comparison of MTA1cMTA9-B–umDNA/hmDNA complexes.
From: Mechanism for the substrate recognition by a eukaryotic DNA N6-adenine methyltransferase complex
a, b Cryo-EM map (a) and structural model (b) of MTA1cMTA9-B–umDNA–SAM complex. c, d Cryo-EM map (c) and structural model (d) of MTA1cMTA9-B–hmDNA–SAM complex. e Structures of MTA1cMTA9-B in complexes with umDNA and hmDNA were superimposed on the MTA1 subunit. The MTA1cMTA9-B–umDNA complex is colored dark gray, while the MTA1cMTA9-B–umDNA complex is colored slate. The pink dash represents the relative movement of p1 NTR. f Conformational difference of DNA molecules in the structural models of MTA1cMTA9-B–umDNA/hmDNA complexes. The pink dash represents the relative motion of two DNA molecules. g High-resolution melting curves of umDNA, hmDNA, and mDNA. Tm values are represented as mean ± SD from independent measurements (n = 3).
