3DEG
Complex of elongating Escherichia coli 70S ribosome and EF4(LepA)-GMPPNP
Summary for 3DEG
| Entry DOI | 10.2210/pdb3deg/pdb |
| EMDB information | 1524 |
| Descriptor | A/L-tRNA, 30S ribosomal protein S12, 50S ribosomal protein L11, ... (11 entities in total) |
| Functional Keywords | ribosome, translation, lepa, ef4, gtp-binding, membrane, nucleotide-binding, antibiotic resistance, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, methylation |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 11 |
| Total formula weight | 190058.63 |
| Authors | Connell, S.R.,Topf, M.,Qin, Y.,Wilson, D.N.,Mielke, T.,Fucini, P.,Nierhaus, K.H.,Spahn, C.M.T. (deposition date: 2008-06-10, release date: 2008-08-19, Last modification date: 2024-03-20) |
| Primary citation | Connell, S.R.,Topf, M.,Qin, Y.,Wilson, D.N.,Mielke, T.,Fucini, P.,Nierhaus, K.H.,Spahn, C.M.T. A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation Nat.Struct.Mol.Biol., 15:910-915, 2008 Cited by PubMed Abstract: EF4 (LepA) is an almost universally conserved translational GTPase in eubacteria. It seems to be essential under environmental stress conditions and has previously been shown to back-translocate the tRNAs on the ribosome, thereby reverting the canonical translocation reaction. In the current work, EF4 was directly visualized in the process of back-translocating tRNAs by single-particle cryo-EM. Using flexible fitting methods, we built a model of ribosome-bound EF4 based on the cryo-EM map and a recently published unbound EF4 X-ray structure. The cryo-EM map establishes EF4 as a noncanonical elongation factor that interacts not only with the elongating ribosome, but also with the back-translocated tRNA in the A-site region, which is present in a previously unseen, intermediate state and deviates markedly from the position of a canonical A-tRNA. Our results, therefore, provide insight into the underlying structural principles governing back-translocation. PubMed: 19172743DOI: 10.1038/nsmb.1469 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (10.9 Å) |
Structure validation
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