4V68
T. thermophilus 70S ribosome in complex with mRNA, tRNAs and EF-Tu.GDP.kirromycin ternary complex, fitted to a 6.4 A Cryo-EM map.
This is a non-PDB format compatible entry.
Summary for 4V68
| Entry DOI | 10.2210/pdb4v68/pdb |
| EMDB information | 5030 |
| Descriptor | 16S rRNA, 30S ribosomal protein S16, 30S ribosomal protein S17, ... (64 entities in total) |
| Functional Keywords | cryo-electron microscopy/elongation factor/gtpase/ribosome/translation, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, metal-binding, zinc-finger, trna-binding, elongation factor, gtp-binding, nucleotide-binding, phosphoprotein, protein biosynthesis, ribosome |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 60 |
| Total formula weight | 2263662.84 |
| Authors | Schuette, J.-C.,Spahn, C.M.T. (deposition date: 2008-12-11, release date: 2014-07-09, Last modification date: 2019-12-18) |
| Primary citation | Schuette, J.C.,Murphy, F.V.,Kelley, A.C.,Weir, J.R.,Giesebrecht, J.,Connell, S.R.,Loerke, J.,Mielke, T.,Zhang, W.,Penczek, P.A.,Ramakrishnan, V.,Spahn, C.M. GTPase activation of elongation factor EF-Tu by the ribosome during decoding Embo J., 28:755-765, 2009 Cited by PubMed Abstract: We have used single-particle reconstruction in cryo-electron microscopy to determine a structure of the Thermus thermophilus ribosome in which the ternary complex of elongation factor Tu (EF-Tu), tRNA and guanine nucleotide has been trapped on the ribosome using the antibiotic kirromycin. This represents the state in the decoding process just after codon recognition by tRNA and the resulting GTP hydrolysis by EF-Tu, but before the release of EF-Tu from the ribosome. Progress in sample purification and image processing made it possible to reach a resolution of 6.4 A. Secondary structure elements in tRNA, EF-Tu and the ribosome, and even GDP and kirromycin, could all be visualized directly. The structure reveals a complex conformational rearrangement of the tRNA in the A/T state and the interactions with the functionally important switch regions of EF-Tu crucial to GTP hydrolysis. Thus, the structure provides insights into the molecular mechanism of signalling codon recognition from the decoding centre of the 30S subunit to the GTPase centre of EF-Tu. PubMed: 19229291DOI: 10.1038/emboj.2009.26 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.4 Å) |
Structure validation
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