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Recognition of amin...
Recognition of aminoacyl-tRNA : a common molecular mechanism revealed by cryo-EM
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- Li, Wen (author)
- Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA
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- Agirrezabala, Xabier (author)
- Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA
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- Lei, Jianlin (author)
- Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA
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- Bouakaz, Lamine (author)
- Uppsala universitet,Molekylärbiologi,ehrenberg
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- Brunelle, Julie L (author)
- Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA
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- Ortiz-Meoz, Rodrigo F (author)
- Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA
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- Green, Rachel (author)
- Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA
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- Sanyal, Suparna (author)
- Uppsala universitet,Molekylärbiologi,sanyal
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- Ehrenberg, Måns (author)
- Uppsala universitet,Molekylärbiologi,ehrenberg
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- Frank, Joachim (author)
- Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA
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(creator_code:org_t)
- 2008-11-20
- 2008
- English.
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In: EMBO Journal. - : Wiley. - 0261-4189 .- 1460-2075. ; 27:24, s. 3322-3331
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Abstract
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- cryo-EM
- decoding
- EF-Tu
- ribosome
- Biology
- Biologi
- Molecular Biology
- Molekylärbiologi
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Li, Wen
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Agirrezabala, Xa ...
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Lei, Jianlin
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Bouakaz, Lamine
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Brunelle, Julie ...
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Ortiz-Meoz, Rodr ...
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show more...
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Green, Rachel
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Sanyal, Suparna
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Ehrenberg, Måns
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Frank, Joachim
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
- Articles in the publication
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EMBO Journal
- By the university
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Uppsala University