5JUO
Saccharomyces cerevisiae 80S ribosome bound with elongation factor eEF2-GDP-sordarin and Taura Syndrome Virus IRES, Structure I (fully rotated 40S subunit)
This is a non-PDB format compatible entry.
Summary for 5JUO
Entry DOI | 10.2210/pdb5juo/pdb |
Related | 5JUP 5JUS 5JUT 5JUU |
EMDB information | 6643 6644 6645 6646 6647 6648 6649 6650 6652 6653 |
Descriptor | 18S ribosomal RNA, eL6 (yeast L6), uL30 (yeast L7), ... (86 entities in total) |
Functional Keywords | 80s-ires, eef2, translocation, sordarin, ribosome |
Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
Total number of polymer chains | 83 |
Total formula weight | 3340490.76 |
Authors | Abeyrathne, P.,Koh, C.S.,Grant, T.,Grigorieff, N.,Korostelev, A.A. (deposition date: 2016-05-10, release date: 2016-10-05, Last modification date: 2019-11-27) |
Primary citation | Abeyrathne, P.D.,Koh, C.S.,Grant, T.,Grigorieff, N.,Korostelev, A.A. Ensemble cryo-EM uncovers inchworm-like translocation of a viral IRES through the ribosome. Elife, 5:-, 2016 Cited by PubMed Abstract: Internal ribosome entry sites (IRESs) mediate cap-independent translation of viral mRNAs. Using electron cryo-microscopy of a single specimen, we present five ribosome structures formed with the Taura syndrome virus IRES and translocase eEF2•GTP bound with sordarin. The structures suggest a trajectory of IRES translocation, required for translation initiation, and provide an unprecedented view of eEF2 dynamics. The IRES rearranges from extended to bent to extended conformations. This inchworm-like movement is coupled with ribosomal inter-subunit rotation and 40S head swivel. eEF2, attached to the 60S subunit, slides along the rotating 40S subunit to enter the A site. Its diphthamide-bearing tip at domain IV separates the tRNA-mRNA-like pseudoknot I (PKI) of the IRES from the decoding center. This unlocks 40S domains, facilitating head swivel and biasing IRES translocation via hitherto-elusive intermediates with PKI captured between the A and P sites. The structures suggest missing links in our understanding of tRNA translocation. PubMed: 27159452DOI: 10.7554/eLife.14874 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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