| http://purl.uniprot.org/citations/35500116 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/35500116 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/35500116 | http://www.w3.org/2000/01/rdf-schema#comment | "Argyrins are a family of naturally produced octapeptides that display promising antimicrobial activity against Pseudomonas aeruginosa. Argyrin B (ArgB) has been shown to interact with an elongated form of the translation elongation factor G (EF-G), leading to the suggestion that argyrins inhibit protein synthesis by interfering with EF-G binding to the ribosome. Here, using a combination of cryo-electron microscopy (cryo-EM) and single-molecule fluorescence resonance energy transfer (smFRET), we demonstrate that rather than interfering with ribosome binding, ArgB rapidly and specifically binds EF-G on the ribosome to inhibit intermediate steps of the translocation mechanism. Our data support that ArgB inhibits conformational changes within EF-G after GTP hydrolysis required for translocation and factor dissociation, analogous to the mechanism of fusidic acid, a chemically distinct antibiotic that binds a different region of EF-G. These findings shed light on the mechanism of action of the argyrin-class antibiotics on protein synthesis as well as the nature and importance of rate-limiting, intramolecular conformational events within the EF-G-bound ribosome during late-steps of translocation."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.2114214119"xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.2114214119"xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Muller R."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Muller R."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Blanchard S.C."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Blanchard S.C."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Osterman I.A."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Osterman I.A."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Rundlet E.J."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Rundlet E.J."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Wilson D.N."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Wilson D.N."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Holm M."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Holm M."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Koller T.O."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Koller T.O."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Morici M."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Morici M."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Pogorevc D."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Pogorevc D."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Maviza T.P."xsd:string |
| http://purl.uniprot.org/citations/35500116 | http://purl.uniprot.org/core/author | "Maviza T.P."xsd:string |