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http://purl.uniprot.org/citations/35064151http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35064151http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35064151http://www.w3.org/2000/01/rdf-schema#comment"EttA, energy-dependent translational throttle A, is a ribosomal factor that gates ribosome entry into the translation elongation cycle. A detailed understanding of its mechanism of action is limited due to the lack of high-resolution structures along its ATPase cycle. Here we present the cryo-electron microscopy (cryo-EM) structures of EttA from Mycobacterium tuberculosis (Mtb), referred to as MtbEttA, in complex with the Mtb 70S ribosome initiation complex (70SIC) at the pre-hydrolysis (ADPNP) and transition (ADP-VO4) states, and the crystal structure of MtbEttA alone in the post-hydrolysis (ADP) state. We observe that MtbEttA binds the E-site of the Mtb 70SIC, remodeling the P-site tRNA and the ribosomal intersubunit bridge B7a during the ribosomal ratcheting. In return, the rotation of the 30S causes conformational changes in MtbEttA, forcing the two nucleotide-binding sites (NBSs) to alternate to engage each ADPNP in the pre-hydrolysis states, followed by complete engagements of both ADP-VO4 molecules in the ATP-hydrolysis transition states. In the post-hydrolysis state, the conserved ATP-hydrolysis motifs of MtbEttA dissociate from both ADP molecules, leaving two nucleotide-binding domains (NBDs) in an open conformation. These structures reveal a dynamic interplay between MtbEttA and the Mtb ribosome, providing insights into the mechanism of translational regulation by EttA-like proteins."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.org/dc/terms/identifier"doi:10.1038/s41467-022-28078-1"xsd:string
http://purl.uniprot.org/citations/35064151http://purl.org/dc/terms/identifier"doi:10.1038/s41467-022-28078-1"xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Cui Z."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Cui Z."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Shin J."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Shin J."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Zhang J."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Zhang J."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Sacchettini J.C."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Sacchettini J.C."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Hou Y.M."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Hou Y.M."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Gamper H."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/author"Gamper H."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/name"Nat. Commun."xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/pages"432"xsd:string
http://purl.uniprot.org/citations/35064151http://purl.uniprot.org/core/pages"432"xsd:string