Cargando…
Cysteine Methylation Controls Radical Generation in the Cfr Radical AdoMet rRNA Methyltransferase
The ‘radical S-adenosyl-L-methionine (AdoMet)’ enzyme Cfr methylates adenosine 2503 of the 23S rRNA in the peptidyltransferase centre (P-site) of the bacterial ribosome. This modification protects host bacteria, notably methicillin-resistant Staphylococcus aureus (MRSA), from numerous antibiotics, i...
Autores principales: | Challand, Martin R., Salvadori, Enrico, Driesener, Rebecca C., Kay, Christopher W. M., Roach, Peter L., Spencer, James |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3702613/ https://www.ncbi.nlm.nih.gov/pubmed/23861844 http://dx.doi.org/10.1371/journal.pone.0067979 |
Ejemplares similares
-
Radical Reaction Control in the AdoMet Radical Enzyme CDG Synthase (QueE): Consolidate, Destabilize, Accelerate
por: Jäger, Christof M., et al.
Publicado: (2016) -
Deconvoluting the Reduction Potentials for the Three
[4Fe-4S] Clusters in an AdoMet Radical SCIFF Maturase
por: Walker, Lindsey M., et al.
Publicado: (2018) -
Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases
por: Mosquera-Rendón, Jeanneth, et al.
Publicado: (2014) -
Enzymatic Generation of Double‐Modified AdoMet Analogues and Their Application in Cascade Reactions with Different Methyltransferases
por: Erguven, Mehmet, et al.
Publicado: (2022) -
Probing a rate-limiting step by mutational perturbation of AdoMet binding in the HhaI methyltransferase
por: Merkienė, Eglė, et al.
Publicado: (2005)