6S0Z
Erythromycin Resistant Staphylococcus aureus 50S ribosome (delta R88 A89 uL22) in complex with erythromycin.
This is a non-PDB format compatible entry.
Summary for 6S0Z
| Entry DOI | 10.2210/pdb6s0z/pdb |
| EMDB information | 10077 |
| Descriptor | 23S ribosomal RNA, 50S ribosomal protein L15, 50S ribosomal protein L16, ... (31 entities in total) |
| Functional Keywords | ribosome, antibiotics, resistance, staphylococcus aureus, exit tunnel, rna, rproteins, erythromycin |
| Biological source | Staphylococcus aureus More |
| Total number of polymer chains | 30 |
| Total formula weight | 1325387.24 |
| Authors | Halfon, Y.,Matozv, D.,Eyal, Z.,Bashan, A.,Zimmerman, E.,Kjeldgaard, J.,Ingmer, H.,Yonath, A. (deposition date: 2019-06-18, release date: 2019-08-21, Last modification date: 2024-10-16) |
| Primary citation | Halfon, Y.,Matzov, D.,Eyal, Z.,Bashan, A.,Zimmerman, E.,Kjeldgaard, J.,Ingmer, H.,Yonath, A. Exit tunnel modulation as resistance mechanism of S. aureus erythromycin resistant mutant. Sci Rep, 9:11460-11460, 2019 Cited by PubMed Abstract: The clinical use of the antibiotic erythromycin (ery) is hampered owing to the spread of resistance genes that are mostly mutating rRNA around the ery binding site at the entrance to the protein exit tunnel. Additional effective resistance mechanisms include deletion or insertion mutations in ribosomal protein uL22, which lead to alterations of the exit tunnel shape, located 16 Å away from the drug's binding site. We determined the cryo-EM structures of the Staphylococcus aureus 70S ribosome, and its ery bound complex with a two amino acid deletion mutation in its ß hairpin loop, which grants the bacteria resistance to ery. The structures reveal that, although the binding of ery is stable, the movement of the flexible shorter uL22 loop towards the tunnel wall creates a wider path for nascent proteins, thus enabling bypass of the barrier formed by the drug. Moreover, upon drug binding, the tunnel widens further. PubMed: 31391518DOI: 10.1038/s41598-019-48019-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.3 Å) |
Structure validation
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