ErmE from Saccharopolyspora erythraea - protein summary.
rRNA adenine N-6-methyltransferase
Erythromycin resistance protein, Macrolide-lincosamide-streptogramin B resistance protein
Position of modification - modification:
The Erm methyltransferases confer resistance to macrolide, lincosamide and streptogramin B (MLS) antibiotics by methylation of a single adenosine base within bacterial 23 S ribosomal RNA. The ErmE methyltransferase, from the macrolide-producing bacterium Saccharopolyspora erythraea, recognizes a motif within domain V of the rRNA that specifically targets adenosine 2058 (A2058) for methylation.
Crystal structure of ErmE - 23S rRNA methyltransferase in macrolide resistance.
Alena Stsiapanava,Maria Selmer
ErmE methyltransferase recognizes features of the primary and secondary structure in a motif within domain V of 23 S rRNA.
I D Villsen,B Vester,S Douthwaite
J Mol Biol
Domain V of 23S rRNA contains all the structural elements necessary for recognition by the ErmE methyltransferase.
B Vester,S Douthwaite
The conformation of 23S rRNA nucleotide A2058 determines its recognition by the ErmE methyltransferase.
B Vester,L H Hansen,S Douthwaite
Copyright © Genesilico - All rights reserved
If you have any advice or suggestions for corrections or improvements, please contact:
Andrea Cappannini -