| Literature DB >> 26552988 |
Laís L Corrêa1, Marta A Witek2, Natalia Zelinskaya2, Renata C Picão3, Graeme L Conn4.
Abstract
The exogenously acquired 16S rRNA methyltransferases RmtD, RmtD2, and RmtG were cloned and heterologously expressed in Escherichia coli, and the recombinant proteins were purified to near homogeneity. Each methyltransferase conferred an aminoglycoside resistance profile consistent with m(7)G1405 modification, and this activity was confirmed by in vitro 30S methylation assays. Analyses of protein structure and interaction with S-adenosyl-l-methionine suggest that the molecular mechanisms of substrate recognition and catalysis are conserved across the 16S rRNA (m(7)G1405) methyltransferase family.Entities:
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Year: 2015 PMID: 26552988 PMCID: PMC4704232 DOI: 10.1128/AAC.02482-15
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191