4v91

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Kluyveromyces lactis 80S ribosome in complex with CrPV-IRES

Structural highlights

4v91 is a 10 chain structure with sequence from Kluyveromyces lactis. This structure supersedes the now removed PDB entries 4cuv and 4cuw. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

The cricket paralysis virus internal ribosome entry site (CrPV-IRES) is a folded structure in a viral mRNA that allows initiation of translation in the absence of any host initiation factors. By using recent advances in single-particle electron cryomicroscopy, we have solved the structure of CrPV-IRES bound to the ribosome of the yeast Kluyveromyces lactis in both the canonical and rotated states at overall resolutions of 3.7 and 3.8 A, respectively. In both states, the pseudoknot PKI of the CrPV-IRES mimics a tRNA/mRNA interaction in the decoding center of the A site of the 40S ribosomal subunit. The structure and accompanying factor-binding data show that CrPV-IRES binding mimics a pretranslocation rather than initiation state of the ribosome. Translocation of the IRES by elongation factor 2 (eEF2) is required to bring the first codon of the mRNA into the A site and to allow the start of translation.

Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome.,Fernandez IS, Bai XC, Murshudov G, Scheres SH, Ramakrishnan V Cell. 2014 May 8;157(4):823-31. doi: 10.1016/j.cell.2014.04.015. Epub 2014 May 1. PMID:24792965[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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References

  1. Fernandez IS, Bai XC, Murshudov G, Scheres SH, Ramakrishnan V. Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome. Cell. 2014 May 8;157(4):823-31. doi: 10.1016/j.cell.2014.04.015. Epub 2014 May 1. PMID:24792965 doi:http://dx.doi.org/10.1016/j.cell.2014.04.015

Contents


4v91, resolution 3.70Å

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