6GZ5
tRNA translocation by the eukaryotic 80S ribosome and the impact of GTP hydrolysis, Translocation-intermediate-POST-3 (TI-POST-3)
This is a non-PDB format compatible entry.
Summary for 6GZ5
| Entry DOI | 10.2210/pdb6gz5/pdb |
| Related | 6GZ3 6GZ4 |
| EMDB information | 0098 0099 0100 |
| Descriptor | 28S ribosomal RNA, ribosomal protein uS19, ribosomal protein uS9, ... (89 entities in total) |
| Functional Keywords | translocation rabbit ribosome, 80s, eef2, head swivel, rotation, ribosome |
| Biological source | Enterobacteria phage SP6 More |
| Total number of polymer chains | 86 |
| Total formula weight | 3325454.94 |
| Authors | Flis, J.,Holm, M.,Rundlet, E.J.,Loerke, J.,Hilal, T.,Dabrowski, M.,Buerger, J.,Mielke, T.,Blanchard, S.C.,Spahn, C.M.T.,Budkevich, T.V. (deposition date: 2018-07-03, release date: 2018-12-05, Last modification date: 2022-03-30) |
| Primary citation | Flis, J.,Holm, M.,Rundlet, E.J.,Loerke, J.,Hilal, T.,Dabrowski, M.,Burger, J.,Mielke, T.,Blanchard, S.C.,Spahn, C.M.T.,Budkevich, T.V. tRNA Translocation by the Eukaryotic 80S Ribosome and the Impact of GTP Hydrolysis. Cell Rep, 25:2676-2688.e7, 2018 Cited by PubMed Abstract: Translocation moves the tRNA⋅mRNA module directionally through the ribosome during the elongation phase of protein synthesis. Although translocation is known to entail large conformational changes within both the ribosome and tRNA substrates, the orchestrated events that ensure the speed and fidelity of this critical aspect of the protein synthesis mechanism have not been fully elucidated. Here, we present three high-resolution structures of intermediates of translocation on the mammalian ribosome where, in contrast to bacteria, ribosomal complexes containing the translocase eEF2 and the complete tRNA⋅mRNA module are trapped by the non-hydrolyzable GTP analog GMPPNP. Consistent with the observed structures, single-molecule imaging revealed that GTP hydrolysis principally facilitates rate-limiting, final steps of translocation, which are required for factor dissociation and which are differentially regulated in bacterial and mammalian systems by the rates of deacyl-tRNA dissociation from the E site. PubMed: 30517857DOI: 10.1016/j.celrep.2018.11.040 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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