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http://purl.uniprot.org/citations/27137929http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27137929http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27137929http://www.w3.org/2000/01/rdf-schema#comment"Elongation factor 4 (EF4) is a member of the family of ribosome-dependent translational GTPase factors, along with elongation factor G and BPI-inducible protein A. Although EF4 is highly conserved in bacterial, mitochondrial, and chloroplast genomes, its exact biological function remains controversial. Here we present the cryo-EM reconstitution of the GTP form of EF4 bound to the ribosome with P and E site tRNAs at 3.8-Å resolution. Interestingly, our structure reveals an unrotated ribosome rather than a clockwise-rotated ribosome, as observed in the presence of EF4-GDP and P site tRNA. In addition, we also observed a counterclockwise-rotated form of the above complex at 5.7-Å resolution. Taken together, our results shed light on the interactions formed between EF4, the ribosome, and the P site tRNA and illuminate the GTPase activation mechanism at previously unresolved detail."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m116.725945"xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Gao Y.G."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Gao Y.G."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Zhan Y."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Zhan Y."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Kumar V."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Kumar V."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Ahmed T."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Ahmed T."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Bhushan S."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Bhushan S."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Ero R."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Ero R."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Goh K.J."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/author"Goh K.J."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/pages"12943-12950"xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/pages"12943-12950"xsd:string
http://purl.uniprot.org/citations/27137929http://purl.uniprot.org/core/title"Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome."xsd:string