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-Structure paper
タイトル | Conformational Differences between Open and Closed States of the Eukaryotic Translation Initiation Complex. |
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ジャーナル・号・ページ | Mol Cell, Vol. 59, Issue 3, Page 399-412, Year 2015 |
掲載日 | 2015年8月6日 |
著者 | Jose L Llácer / Tanweer Hussain / Laura Marler / Colin Echeverría Aitken / Anil Thakur / Jon R Lorsch / Alan G Hinnebusch / V Ramakrishnan / |
PubMed 要旨 | Translation initiation in eukaryotes begins with the formation of a pre-initiation complex (PIC) containing the 40S ribosomal subunit, eIF1, eIF1A, eIF3, ternary complex (eIF2-GTP-Met-tRNAi), and ...Translation initiation in eukaryotes begins with the formation of a pre-initiation complex (PIC) containing the 40S ribosomal subunit, eIF1, eIF1A, eIF3, ternary complex (eIF2-GTP-Met-tRNAi), and eIF5. The PIC, in an open conformation, attaches to the 5' end of the mRNA and scans to locate the start codon, whereupon it closes to arrest scanning. We present single particle cryo-electron microscopy (cryo-EM) reconstructions of 48S PICs from yeast in these open and closed states, at 6.0 Å and 4.9 Å, respectively. These reconstructions show eIF2β as well as a configuration of eIF3 that appears to encircle the 40S, occupying part of the subunit interface. Comparison of the complexes reveals a large conformational change in the 40S head from an open mRNA latch conformation to a closed one that constricts the mRNA entry channel and narrows the P site to enclose tRNAi, thus elucidating key events in start codon recognition. |
リンク | Mol Cell / PubMed:26212456 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.46 - 14.9 Å |
構造データ | EMDB-3047: 40S-eIF1A-eIF1 complex EMDB-3048, PDB-3jap: EMDB-3049: EMDB-3050: |
化合物 | ChemComp-MG: ChemComp-ZN: ChemComp-MET: ChemComp-GCP: |
由来 |
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キーワード | TRANSLATION / Eukaryotic translation initiation / 48S / small ribosome subunit / 40S / 43S |