Figure 3: Superimposition of various antibiotics relative to ErmBL. | Nature Communications

Figure 3: Superimposition of various antibiotics relative to ErmBL.

From: Molecular basis for erythromycin-dependent ribosome stalling during translation of the ErmBL leader peptide

Figure 3

(a) Detection of ribosome stalling by toe-printing during translation of ermBL, in the presence of the antibiotics erythromycin (ERY), ITR-054 (054), oleandomycin (OLE), solithromycin (SOL), azithromycin (AZM), josamycin (JOS), clindamycin (CLN) and quinupristin (QUI). The arrowed toe-print band indicates that ErmBL arrests translation with the Asp (D10) codon (boxed) located in the P-site. (b) Chemical structures of ERY, macrolides ITR-054 (054), OLE, the ketolide SOL and the azalide AZM compared with the macrolide JOS, the lincosamide CLN and the streptogramin B QUI. Differences between ERY and respective drugs are highlighted. (c) ErmBL-SRC map (grey mesh) with molecular model for ErmBL-tRNA (teal), 23S rRNA (blue) and ERY (red, PDB3OFR11). (d–h) as in (c), but with relative binding positions of (d) AZM (green, PDB1M1K19), (e) SOL (yellow, PDB3ORB42), (f) JOS (purple, PDB2O44), (g) CLN (orange, PDB3OFZ11) and (h) QUI (pink, PDB1SM1 (ref. 20)20).

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