EC Number   |
|---|
   2.1.1.348 | crystal structures of the complex of Mettl3/Mettl14 methyltransferase domains in apo form as well as with bound S-adenosylmethionine (SAM) or S-adenosylhomocysteine (SAH) in the catalytic site. The heterodimeric complex of methyltransferase domains, combined with CCCH motifs constitute the minimally required regions for creating m6A modifications in vitro. Mettl3 is the catalytically active subunit while Mettl14 plays a structural role critical for substrate recognition |
| 2.1.1.348 | crystal structures of the METTL3-METTL14 heterodimer with methyltransferase domains in the ligand-free, S-adenosyl methionine (AdoMet-)bound and S-adenosyl homocysteine (AdoHcy-)bound states, with resolutions of 1.9, 1.71 and 1.61 A, respectively. Both METTL3 and METTL14 adopt a class I methyltransferase fold and they interact with each other via an extensive hydrogen bonding network, generating a positively charged groove |
| 2.1.1.348 | sitting drop vapor diffusion method, using 18% (w/v) PEG 8000 and 0.1 M sodium citrate, pH 5.7 |
| 2.1.1.348 | solution structure for the zinc finger domain of catalytic subunit METTL3. The zinc finger domain specifically binds to an RNA containing 5'-GGACU-3' consensus sequence. The zinc finger domain contains two CCCH-type zinc fingers connected by an anti-parallel beta-sheet. The RNA-binding interface comprises basic residues from zinc finger 1 and hydrophobic residues from beta-sheet and zinc finger 2 |
