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TitleA new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 15, Issue 9, Page 910-915, Year 2008
Publish dateFeb 19, 2009
AuthorsSean R Connell / Maya Topf / Yan Qin / Daniel N Wilson / Thorsten Mielke / Paola Fucini / Knud H Nierhaus / Christian M T Spahn /
PubMed AbstractEF4 (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 ...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.
External linksNat Struct Mol Biol / PubMed:19172743
MethodsEM (single particle)
Resolution10.9 Å
Structure data

1524

3deg

EMDB-1524, PDB-3deg:
Complex of elongating Escherichia coli 70S ribosome and EF4(LepA)-GMPPNP
Method: EM (single particle) / Resolution: 10.9 Å

Source
  • escherichia coli (E. coli)
KeywordsRIBOSOME / translation / LepA / EF4 / GTP-binding / Membrane / Nucleotide-binding / Antibiotic resistance / Ribonucleoprotein / Ribosomal protein / RNA-binding / rRNA-binding / tRNA-binding / Methylation

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