Formation of the First Peptide Bond: The Structure of EF-P Bound to the 70 <i>S</i> Ribosome
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- Gregor Blaha
- Departments of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
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- Robin E. Stanley
- Departments of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
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- Thomas A. Steitz
- Departments of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
書誌事項
- 公開日
- 2009-08-21
- DOI
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- 10.1126/science.1175800
- 公開者
- American Association for the Advancement of Science (AAAS)
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説明
<jats:title>Protein Synthesis Initiation Complex</jats:title> <jats:p> The final step in the initiation phase of protein synthesis is the formation of the first peptide bond, which requires initiator transfer RNA (tRNA) to be bound at the ribosomal P site. Elongation factor P (EF-P) is a protein conserved in all eubacteria that stimulates this initial bond formation. Insight into how this is achieved comes from a structure of <jats:italic>Thermus thermophilus</jats:italic> 70 <jats:italic>S</jats:italic> ribosome bound to EF-P, initiator tRNA, and a short piece of messenger RNA presented by <jats:bold> Blaha <jats:italic>et al.</jats:italic> </jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" page="966" related-article-type="in-this-issue" vol="325" xlink:href="10.1126/science.1175800">966</jats:related-article> ). EF-P binds between the P and E sites and facilitates proper positioning of initiator tRNA in the P site. A similar mechanism is likely to apply to structurally homologous initiation factors in archea and eukarya. </jats:p>
収録刊行物
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- Science
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Science 325 (5943), 966-970, 2009-08-21
American Association for the Advancement of Science (AAAS)
