| Structural highlights
Function
NPMA_ECOLX Specifically methylates the N(1) position of adenine 1408 in 16S rRNA. Confers resistance to various aminoglycosides, including kanamycin, neomycin, apramycin, ribostamycin and gentamicin. Methylates only fully assembled 30S subunits.[1] [2] [3]
References
- ↑ Wachino J, Shibayama K, Kurokawa H, Kimura K, Yamane K, Suzuki S, Shibata N, Ike Y, Arakawa Y. Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides. Antimicrob Agents Chemother. 2007 Dec;51(12):4401-9. Epub 2007 Sep 17. PMID:17875999 doi:https://dx.doi.org/10.1128/AAC.00926-07
- ↑ Zelinskaya N, Rankin CR, Macmaster R, Savic M, Conn GL. Expression, purification and crystallization of adenosine 1408 aminoglycoside-resistance rRNA methyltransferases for structural studies. Protein Expr Purif. 2011 Jan;75(1):89-94. doi: 10.1016/j.pep.2010.07.005. Epub, 2010 Jul 25. PMID:20667473 doi:https://dx.doi.org/10.1016/j.pep.2010.07.005
- ↑ Husain N, Obranic S, Koscinski L, Seetharaman J, Babic F, Bujnicki JM, Maravic-Vlahovicek G, Sivaraman J. Structural basis for the methylation of A1408 in 16S rRNA by a panaminoglycoside resistance methyltransferase NpmA from a clinical isolate and analysis of the NpmA interactions with the 30S ribosomal subunit. Nucleic Acids Res. 2010 Nov 9. PMID:21062819 doi:10.1093/nar/gkq1033
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