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6GZ4

tRNA translocation by the eukaryotic 80S ribosome and the impact of GTP hydrolysis, Translocation-intermediate-POST-2 (TI-POST-2)

This is a non-PDB format compatible entry.
Summary for 6GZ4
Entry DOI10.2210/pdb6gz4/pdb
Related6GZ3 6GZ5
EMDB information0098 0099 0100
Descriptorribosomal protein uL2, pe/E-site-tRNA, 18S ribosomal RNA, ... (89 entities in total)
Functional Keywordstranslocation, mammalian, 80s, eef2, ef-g, gmppnp, dde, diphthamide, ribosome
Biological sourceOryctolagus cuniculus
More
Total number of polymer chains86
Total formula weight3325454.94
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 citationFlis, 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: 30517857
DOI: 10.1016/j.celrep.2018.11.040
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

226707

数据于2024-10-30公开中

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