4V3P
The molecular structure of the left-handed supra-molecular helix of eukaryotic polyribosomes
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Summary for 4V3P
Entry DOI | 10.2210/pdb4v3p/pdb |
EMDB information | 2790 |
Descriptor | G protein beta subunit, 40S ribosomal protein S23, 40S ribosomal protein S18, ... (84 entities in total) |
Functional Keywords | ribosome |
Biological source | Triticum aestivum (bread wheat) More |
Total number of polymer chains | 87 |
Total formula weight | 3001444.59 |
Authors | Myasnikov, A.G.,Afonina, Z.A.,Menetret, J.F.,Shirokov, V.A.,Spirin, A.S.,Klaholz, B.P. (deposition date: 2014-10-20, release date: 2015-04-22, Last modification date: 2019-12-18) |
Primary citation | Myasnikov, A.G.,Afonina, Z.A.,Menetret, J.F.,Shirokov, V.A.,Spirin, A.S.,Klaholz, B.P. The molecular structure of the left-handed supra-molecular helix of eukaryotic polyribosomes. Nat Commun, 5:5294-5294, 2014 Cited by PubMed Abstract: During protein synthesis, several ribosomes bind to a single messenger RNA (mRNA) forming large macromolecular assemblies called polyribosomes. Here we report the detailed molecular structure of a 100 MDa eukaryotic poly-ribosome complex derived from cryo electron tomography, sub-tomogram averaging and pseudo-atomic modelling by crystal structure fitting. The structure allowed the visualization of the three functional parts of the polysome assembly, the central core region that forms a rather compact left-handed supra-molecular helix, and the more open regions that harbour the initiation and termination sites at either ends. The helical region forms a continuous mRNA channel where the mRNA strand bridges neighbouring exit and entry sites of the ribosomes and prevents mRNA looping between ribosomes. This structure provides unprecedented insights into protein- and RNA-mediated inter-ribosome contacts that involve conserved sites through 40S subunits and long protruding RNA expansion segments, suggesting a role in stabilizing the overall polyribosomal assembly. PubMed: 25376914DOI: 10.1038/ncomms6294 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (34 Å) |
Structure validation
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