Fig. 3: Structural details of TthMTA1-Tthp1-Tthp2 and TthMTA1-PteMTA9 intermolecular contacts.
From: Structural basis for MTA1c-mediated DNA N6-adenine methylation
a Detailed interactions between MTA1 and p2, as well as between MTA1 and p1 in the MTA1-p1-p2 complex. b GST pull-down experiments assaying the ability of GST-p2 mutants to interact with MTA1. MTA1 proteins were incubated with wild-type or mutant GST-p2 proteins immobilized on glutathione resin. The bound MTA1 proteins were quantitatively analyzed by the gray scanning. c GST pull-down experiments assaying the ability of MTA1 mutants to interact with GST-P2. d GST pull-down experiments assaying the ability of GST-p1 mutants to interact with MTA1. e Sequence alignments of hydrophobic α helices in the MTA1 (left panel) and p1 (right panel) proteins. Each sequence is labeled with its GenBank Identifier (GI) number and the systematic name of an organism. The conserved hydrophobic residues are shaded in red. f Detailed interactions between MTA1 and MTA9 in the MTA1-MTA9 complex. g GST pull-down experiments assaying the ability of GST-MTA1 (residues 171–372) mutants to interact with MTA9. h GST pull-down experiments assaying the ability of MTA9 mutants to interact with GST-MTA1 (residues 171-372). Source data for (b–d, g–h) are provided in a Source Data file.
