4w2e

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Crystal structure of Elongation Factor 4 (EF4/LepA) bound to the Thermus thermophilus 70S ribosome

Structural highlights

4w2e is a 10 chain structure with sequence from Thermus thermophilus and Thermus thermophilus HB8. This structure supersedes the now removed PDB entries 4qjs and 4qjt. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:4SU, 5MU, 7MG, F3O, GDP, MG, MIA, PSU, SF4, ZN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL2_THET8 One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial (By similarity). Makes several contacts with the 16S rRNA (forming bridge B7b) in the 70S ribosome.[HAMAP-Rule:MF_01320_B]

Publication Abstract from PubMed

Elongation factor 4 (EF4/LepA) is a highly conserved guanosine triphosphatase translation factor. It was shown to promote back-translocation of tRNAs on posttranslocational ribosome complexes and to compete with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis. Here, we report a crystal structure of EF4-guanosine diphosphate bound to the Thermus thermophilus ribosome with a P-site tRNA at 2.9 angstroms resolution. The C-terminal domain of EF4 reaches into the peptidyl transferase center and interacts with the acceptor stem of the peptidyl-tRNA in the P site. The ribosome is in an unusual state of ratcheting with the 30S subunit rotated clockwise relative to the 50S subunit, resulting in a remodeled decoding center. The structure is consistent with EF4 functioning either as a back-translocase or a ribosome sequester.

Ribosome structure. Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome.,Gagnon MG, Lin J, Bulkley D, Steitz TA Science. 2014 Aug 8;345(6197):684-7. doi: 10.1126/science.1253525. PMID:25104389[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
3 reviews cite this structure
Mechanisms of ribosome rescue in bacteria.
Keiler et al. (2015)
2 more
20 other articles
No citations found

See Also

References

  1. ↑ Gagnon MG, Lin J, Bulkley D, Steitz TA. Ribosome structure. Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. Science. 2014 Aug 8;345(6197):684-7. doi: 10.1126/science.1253525. PMID:25104389 doi:http://dx.doi.org/10.1126/science.1253525

Contents


PDB ID 4w2e

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