Crystal Structure of ErmC‘, an rRNA Methyltransferase Which Mediates Antibiotic Resistance in Bacteria

The prevalent mechanism of bacterial resistance to erythromycin and other antibiotics of the macrolide−lincosamide−streptogramin B group (MLS) is methylation of the 23S rRNA component of the 50S subunit in bacterial ribosomes. This sequence-specific methylation is catalyzed by the Erm group of methy...

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Veröffentlicht in:	Biochemistry (Easton) 1998-05, Vol.37 (20), p.7103-7112
Hauptverfasser:	Bussiere, Dirksen E, Muchmore, Steven W, Dealwis, Christopher G, Schluckebier, Gerd, Nienaber, Vicki L, Edalji, Rohinton P, Walter, Karl A, Ladror, Uri S, Holzman, Thomas F, Abad-Zapatero, Cele
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anti-Bacterial Agents - pharmacology Bacillus subtilis Bacillus subtilis - drug effects Bacillus subtilis - enzymology Base Sequence Crystallography, X-Ray Drug Resistance, Microbial Lincosamides Macrolides Methyltransferases - chemistry Models, Molecular Molecular Sequence Data Protein Binding RNA, Ribosomal - metabolism S-Adenosylhomocysteine - metabolism Virginiamycin - pharmacology
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