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http://purl.uniprot.org/citations/31189921http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31189921http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31189921http://www.w3.org/2000/01/rdf-schema#comment"When the ribosome encounters a stop codon, it recruits a release factor (RF) to hydrolyze the ester bond between the peptide chain and tRNA. RFs have structural motifs that recognize stop codons in the decoding center and a GGQ motif for induction of hydrolysis in the peptidyl transfer center 70 Å away. Surprisingly, free RF2 is compact, with only 20 Å between its codon-reading and GGQ motifs. Cryo-EM showed that ribosome-bound RFs have extended structures, suggesting that RFs are compact when entering the ribosome and then extend their structures upon stop codon recognition. Here we use time-resolved cryo-EM to visualize transient compact forms of RF1 and RF2 at 3.5 and 4 Å resolution, respectively, in the codon-recognizing ribosome complex on the native pathway. About 25% of complexes have RFs in the compact state at 24 ms reaction time, and within 60 ms virtually all ribosome-bound RFs are transformed to their extended forms."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.org/dc/terms/identifier"doi:10.1038/s41467-019-10608-z"xsd:string
http://purl.uniprot.org/citations/31189921http://purl.org/dc/terms/identifier"doi:10.1038/s41467-019-10608-z"xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Chen B."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Chen B."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Frank J."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Frank J."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Fu Z."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Fu Z."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Sun M."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Sun M."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Indrisiunaite G."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Indrisiunaite G."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Shah B."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Shah B."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Grassucci R.A."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Grassucci R.A."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Ehrenberg M."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Ehrenberg M."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Kaledhonkar S."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/author"Kaledhonkar S."xsd:string
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31189921http://purl.uniprot.org/core/date"2019"xsd:gYear