EC Number   |
|---|
    2.1.1.37 | crystal structure of the cytosine-5-methyltransferase EhMeth at a resolution of 2.15 A is presented in complex with its reaction product S-adenosyl-L-homocysteine. In contrast to the human DNMT2 structure, the active site loop (residues 80-100) of EhMeth is well defined and clearly forms an alpha-helix |
| 2.1.1.37 | crystal structures of HhaI methyltransferase complexed with cognate unmethylated or methylated DNA together with S-adenosyl-L-homocysteine |
| 2.1.1.37 | molecular dynamics simulations. The free energy profiles for the flipping of target cytosine into the enzyme active site support the major groove base eversion pathway. The closed state of enzyme increases the free energy barrier, whereas the open state reduces it. The interactions of the key loop residues of protein with cognate DNA alter the protein motions, and modulation of protein fluctuations relates to the closed catalytic complex formation. Methylation of cytosine in the active site of the closed complex destabilizes the interactions of catalytic loop residues with cognate DNA and reduces the stability of the closed state |
| 2.1.1.37 | small-angle X-ray scattering reveals two distinct protein domains of unequal size. The larger domain matches the crystallographic structure of DNA methyltransferase HhaI, and the cleft in this domain is occupied by DNA in the model. Homology modeling represents the N-terminal region either as a flexible chain of dummy residues or as a rigid structure of a homologous protein connected to the methyltransferase domain by a short flexible linker. Both models demonstrate high mobility of the N-terminal region |
| 2.1.1.37 | structure-based model of the M.HhaI-DNA-cofactor complex. Residues Gln82, Tyr254 and Asn304 are in close proximity and thus might sterically interfere with the extended transferable side chains |
