23S rRNA (adenine2085-N6)-dimethyltransferase
Substrate requirements for ErmC' methyltransferase activity.
Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance.
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-244
Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria.
Novel inhibitors of Erm methyltransferases from NMR and parallel synthesis.
The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism.
Crystal structure of the transcription factor sc-mtTFB offers insights into mitochondrial transcription.
Identification of essential residues in the Erm(B) rRNA methyltransferase of Clostridium perfringens.
Sequence analysis and structure prediction of 23S rRNA:m1G methyltransferases reveals a conserved core augmented with a putative Zn-binding domain in the N-terminus and family-specific elaborations in the C-terminus.
Mutational analysis defines the roles of conserved amino acid residues in the predicted catalytic pocket of the rRNA:m6A methyltransferase ErmC'.
Mutational analysis of basic residues in the N-terminus of the rRNA:m6A methyltransferase ErmC'.
Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli.
Structural and functional characterization of CFE88: evidence that a conserved and essential bacterial protein is a methyltransferase.
According to the literature [9], the catalytic residues of this enzyme is nearly the same as that of Modification methylase TaqI (D00080 in EzCatDB), suggesting that it has a similar mechanism to that.