Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria

By F. Schluenzen, R. Zarivach, J. Harms, A. Bashan, A. Tocilj, Renate Albrecht, A. Yonath, F. Franceschi. Nature, 2001

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Identifying the methyltransferases for m5U747 and m5U1939 in 23S rRNA using MALDI mass spectrometry (2003, background): “synthesis (3, 5 ). This region of the tunnel additionally forms a binding pocket for macrolides and other antibiotics (39,46,47).”
Molecular basis of bacterial resistance to chloramphenicol and florfenicol. (2004, background): “Its bacteriostatic activity is based on a reversible binding to the peptidyltransferase centre at the 50S ribosomal subunit of 70S ribosomes [10].”
The non-Watson-Crick base pairs and their associated isostericity matrices. (2002, background): “radiodurans (49) TRNA07 Yeast tRNA (ASP) (8) TRNA09 Yeast tRNA (PHE) (8)”
The Cfr rRNA Methyltransferase Confers Resistance to Phenicols, Lincosamides, Oxazolidinones, Pleuromutilins, and Streptogramin A Antibiotics (2006, background): “The crystal structures of bound chloramphenicol, clindamycin, tiamulin, and dalfopristin (4, 20, 21) show that they bind to overlapping sites at the peptidyl transferase site at the entrance of the ribosomal exit tunnel (Fig.”
Bacterial resistance to antibiotics: enzymatic degradation and modification. (2005, background): “8) that interacts directly with the 23S rRNA [64].”