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Literature summary for 2.3.2.12 extracted from

  • Wilson, D.N.; Schluenzen, F.; Harms, J.M.; Starosta, A.L.; Connell, S.R.; Fucini, P.
    The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning (2008), Proc. Natl. Acad. Sci. USA, 105, 13339-13344.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the inhibitor linezolid bound to the 50S ribosomal subunit. Linezolid binds in the A site pocket at the peptidyltransferase center of the ribosome overlapping the aminoacyl moiety of an A-site bound tRNA as well as many clinically important antibiotics. Binding of linezolid stabilizes a distinct conformation of the universally conserved 23S rRNA nucleotide U2585 that would be nonproductive for peptide bond formation. In a model oxazolidinones impart their inhibitory effect by perturbing the correct positioning of tRNAs on the ribosome Deinococcus radiodurans

Inhibitors

Inhibitors Comment Organism Structure
linezolid binds in the A site pocket at the peptidyltransferase center of the ribosome overlapping the aminoacyl moiety of an A-site bound tRNA as well as many clinically important antibiotics. Binding of linezolid stabilizes a distinct conformation of the universally conserved 23S rRNA nucleotide U2585 that would be nonproductive for peptide bond formation. In a model oxazolidinones impart their inhibitory effect by perturbing the correct positioning of tRNAs on the ribosome Deinococcus radiodurans

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans
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