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Science. 2014 Aug 8;345(6197):684-7. doi: 10.1126/science.1253525.

Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome.

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA. Howard Hughes Medical Institute, Yale University, New Haven, CT 06520-8114, USA.
2
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
3
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA. Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA.
4
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA. Howard Hughes Medical Institute, Yale University, New Haven, CT 06520-8114, USA. Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA. thomas.steitz@yale.edu.

Abstract

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.

PMID:
25104389
DOI:
10.1126/science.1253525
[Indexed for MEDLINE]
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