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Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA.
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA.
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular Biology. (ehrenberg)
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2008 (English)In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 27, no 24, 3322-3331 p.Article in journal (Refereed) Published
Abstract [en]

The accuracy of ribosomal translation is achieved by an initial selection and a proofreading step, mediated by EF-Tu, which forms a ternary complex with aminoacyl(aa)-tRNA. To study the binding modes of different aa-tRNAs, we compared cryo-EM maps of the kirromycin-stalled ribosome bound with ternary complexes containing Phe-tRNA(Phe), Trp-tRNA(Trp), or Leu-tRNA(LeuI). The three maps suggest a common binding manner of cognate aa-tRNAs in their specific binding with both the ribosome and EF-Tu. All three aa-tRNAs have the same 'loaded spring' conformation with a kink and twist between the D-stem and anticodon stem. The three complexes are similarly integrated in an interaction network, extending from the anticodon loop through h44 and protein S12 to the EF-Tu-binding CCA end of aa-tRNA, proposed to signal cognate codon-anticodon interaction to the GTPase centre and tune the accuracy of aa-tRNA selection.

Place, publisher, year, edition, pages
2008. Vol. 27, no 24, 3322-3331 p.
Keyword [en]
cryo-EM, decoding, EF-Tu, ribosome
National Category
Biological Sciences
Research subject
Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-104041DOI: 10.1038/emboj.2008.243ISI: 000261785900010PubMedID: 19020518OAI: oai:DiVA.org:uu-104041DiVA: diva2:219279
Available from: 2009-05-27 Created: 2009-05-27 Last updated: 2017-12-13Bibliographically approved

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