Fig. 3: Structure and interactions of the dimeric methyltransferase MtrH.
A Overview of MtrH positioning in the Mtr complex. Cartoon representation of dimeric MtrH bound to one protomer of the stalk-forming MtrABFG helix-bundle. The rest of the complex is depicted as a white, semi-transparent surface. B Close-up view of the extended ß-sheet formed by the N-termini of MtrBFG and the MtrH-stalk interface created by the MtrB sheet. C MtrH-MtrB interface. Residues involved in hydrophobic and charged interactions are labelled and shown as sticks. D Conservation of MtrB-MtrH interacting residues across Methanoarchaea. E Conservation of substrate-binding residues within the MtrH active site across Methanoarchaea. F Superposition of MtrH (light and dark blue) and MtgA (PDB: 6SJN, green). G Close-up of the superposition of the active site of MtrH and MtgA. Residues involved or potentially involved in substrate-binding, as well as Methyltetrahydrofolate (mH4F) and H4MPT, are shown as sticks. The density of mH4F (green) bound to MtgA was used to model the binding of H4MPT (purple, grey, orange).
