Summary for 7NHM
| Entry DOI | 10.2210/pdb7nhm/pdb |
| EMDB information | 12333 |
| Descriptor | 50S ribosomal protein L27, 50S ribosomal protein L6, 50S ribosomal protein L13, ... (56 entities in total) |
| Functional Keywords | protein synthesis, ribosome, initiation |
| Biological source | Staphylococcus aureus subsp. aureus NCTC 8325 More |
| Total number of polymer chains | 52 |
| Total formula weight | 2167794.39 |
| Authors | Crowe-McAuliffe, C.,Murina, V.,Hauryliuk, V.,Wilson, D.N. (deposition date: 2021-02-10, release date: 2021-05-05, Last modification date: 2024-05-01) |
| Primary citation | Crowe-McAuliffe, C.,Murina, V.,Turnbull, K.J.,Kasari, M.,Mohamad, M.,Polte, C.,Takada, H.,Vaitkevicius, K.,Johansson, J.,Ignatova, Z.,Atkinson, G.C.,O'Neill, A.J.,Hauryliuk, V.,Wilson, D.N. Structural basis of ABCF-mediated resistance to pleuromutilin, lincosamide, and streptogramin A antibiotics in Gram-positive pathogens. Nat Commun, 12:3577-3577, 2021 Cited by PubMed Abstract: Target protection proteins confer resistance to the host organism by directly binding to the antibiotic target. One class of such proteins are the antibiotic resistance (ARE) ATP-binding cassette (ABC) proteins of the F-subtype (ARE-ABCFs), which are widely distributed throughout Gram-positive bacteria and bind the ribosome to alleviate translational inhibition from antibiotics that target the large ribosomal subunit. Here, we present single-particle cryo-EM structures of ARE-ABCF-ribosome complexes from three Gram-positive pathogens: Enterococcus faecalis LsaA, Staphylococcus haemolyticus VgaA and Listeria monocytogenes VgaL. Supported by extensive mutagenesis analysis, these structures enable a general model for antibiotic resistance mediated by these ARE-ABCFs to be proposed. In this model, ABCF binding to the antibiotic-stalled ribosome mediates antibiotic release via mechanistically diverse long-range conformational relays that converge on a few conserved ribosomal RNA nucleotides located at the peptidyltransferase center. These insights are important for the future development of antibiotics that overcome such target protection resistance mechanisms. PubMed: 34117249DOI: 10.1038/s41467-021-23753-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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