| http://purl.uniprot.org/citations/34117249 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/34117249 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/34117249 | http://www.w3.org/2000/01/rdf-schema#comment | "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 VgaALC 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."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-021-23753-1"xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-021-23753-1"xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Takada H."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Takada H."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Wilson D.N."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Wilson D.N."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Ignatova Z."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Ignatova Z."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Johansson J."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Johansson J."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Atkinson G.C."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Atkinson G.C."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Hauryliuk V."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Hauryliuk V."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Kasari M."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Kasari M."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Murina V."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Murina V."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "O'Neill A.J."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "O'Neill A.J."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Crowe-McAuliffe C."xsd:string |
| http://purl.uniprot.org/citations/34117249 | http://purl.uniprot.org/core/author | "Crowe-McAuliffe C."xsd:string |