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-Structure paper
タイトル | Molecular architecture of a eukaryotic translational initiation complex. |
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ジャーナル・号・ページ | Science, Vol. 342, Issue 6160, Page 1240585, Year 2013 |
掲載日 | 2013年11月15日 |
著者 | Israel S Fernández / Xiao-Chen Bai / Tanweer Hussain / Ann C Kelley / Jon R Lorsch / V Ramakrishnan / Sjors H W Scheres / |
PubMed 要旨 | The last step in eukaryotic translational initiation involves the joining of the large and small subunits of the ribosome, with initiator transfer RNA (Met-tRNA(i)(Met)) positioned over the start ...The last step in eukaryotic translational initiation involves the joining of the large and small subunits of the ribosome, with initiator transfer RNA (Met-tRNA(i)(Met)) positioned over the start codon of messenger RNA in the P site. This step is catalyzed by initiation factor eIF5B. We used recent advances in cryo-electron microscopy (cryo-EM) to determine a structure of the eIF5B initiation complex to 6.6 angstrom resolution from <3% of the population, comprising just 5143 particles. The structure reveals conformational changes in eIF5B, initiator tRNA, and the ribosome that provide insights into the role of eIF5B in translational initiation. The relatively high resolution obtained from such a small fraction of a heterogeneous sample suggests a general approach for characterizing the structure of other dynamic or transient biological complexes. |
リンク | Science / PubMed:24200810 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.3 - 6.6 Å |
構造データ | |
化合物 | ChemComp-ZN: ChemComp-MG: ChemComp-OHX: ChemComp-GCP: |
由来 |
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キーワード | RIBOSOME / RIBOSOME INITIATION COMPLEX / INITIATOR FACTOR EIF5B / SINGLE PARTICLE ANALYSIS |