23S rRNA (adenine2085-N6)-dimethyltransferase

23S rRNA (adenine2085-N6)-dimethyltransferase (EC 2.1.1.184, ErmC' methyltransferase, ermC methylase, ermC 23S rRNA methyltransferase, rRNA:m6A methyltransferase ErmC', ErmC', rRNA methyltransferase ErmC' ) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2085-N6)-dimethyltransferase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA 2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA
23S rRNA (adenine2085-N6)-dimethyltransferase
Identifiers
EC number2.1.1.184
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalysing the methylation of 23S rRNA at adenine2085.

References
  1. Zhong P, Pratt SD, Edalji RP, Walter KA, Holzman TF, Shivakumar AG, Katz L (August 1995). "Substrate requirements for ErmC' methyltransferase activity". Journal of Bacteriology. 177 (15): 4327–32. PMC 177180. PMID 7543473.
  2. Denoya C, Dubnau D (February 1989). "Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase". The Journal of Biological Chemistry. 264 (5): 2615–24. PMID 2492520.
  3. Denoya CD, Dubnau D (August 1987). "Site and substrate specificity of the ermC 23S rRNA methyltransferase". Journal of Bacteriology. 169 (8): 3857–60. PMC 212483. PMID 2440853.
  4. Bussiere DE, Muchmore SW, Dealwis CG, Schluckebier G, Nienaber VL, Edalji RP, Walter KA, Ladror US, Holzman TF, Abad-Zapatero C (May 1998). "Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria". Biochemistry. 37 (20): 7103–12. doi:10.1021/bi973113c. PMID 9585521.
  5. Schluckebier G, Zhong P, Stewart KD, Kavanaugh TJ, Abad-Zapatero C (June 1999). "The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism". Journal of Molecular Biology. 289 (2): 277–91. doi:10.1006/jmbi.1999.2788. PMID 10366505.
  6. Maravić G, Bujnicki JM, Feder M, Pongor S, Flögel M (August 2003). "Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions". Nucleic Acids Research. 31 (16): 4941–9. doi:10.1093/nar/gkg666. PMC 169915. PMID 12907737.
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