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-Structure paper
タイトル | Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy. |
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ジャーナル・号・ページ | Nat Struct Biol, Vol. 10, Issue 11, Page 899-906, Year 2003 |
掲載日 | 2003年10月19日 |
著者 | Mikel Valle / Andrey Zavialov / Wen Li / Scott M Stagg / Jayati Sengupta / Rikke C Nielsen / Poul Nissen / Stephen C Harvey / Måns Ehrenberg / Joachim Frank / |
PubMed 要旨 | Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa-tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, ...Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa-tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, at a resolution of approximately 9 A, showing that during the incorporation of the aa-tRNA into the 70S ribosome of Escherichia coli, the flexibility of aa-tRNA allows the initial codon recognition and its accommodation into the ribosomal A site. In addition, a conformational change observed in the GTPase-associated center (GAC) of the ribosomal 50S subunit may provide the mechanism by which the ribosome promotes a relative movement of the aa-tRNA with respect to EF-Tu. This relative rearrangement seems to facilitate codon recognition by the incoming aa-tRNA, and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu. From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome. |
リンク | Nat Struct Biol / PubMed:14566331 |
手法 | EM (単粒子) |
解像度 | 9.0 - 12.8 Å |
構造データ | EMDB-1055: Locking and unlocking of ribosomal motions. EMDB-1056: Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy. EMDB-1395: |
由来 |
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キーワード | RNA / tRNA model / decoding / A/T-site tRNA. / A-site tRNA / RNA Binding Protein/RNA / ribosomal protein / rRNA / RNA Binding Protein-RNA COMPLEX / BIOSYNTHETIC PROTEIN / Elongation factor |