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

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.

Authors:
; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1354313
Report Number(s):
BNL-112829-2016-JA
Journal ID: ISSN 0036-8075
DOE Contract Number:  
SC00112704
Resource Type:
Journal Article
Journal Name:
Science
Additional Journal Information:
Journal Volume: 345; Journal Issue: 6197; Journal ID: ISSN 0036-8075
Publisher:
AAAS
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES

Citation Formats

Gagnon, M. G., Lin, J., Bulkley, D., and Steitz, T. A. Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. United States: N. p., 2014. Web. doi:10.1126/science.1253525.
Gagnon, M. G., Lin, J., Bulkley, D., & Steitz, T. A. Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. United States. doi:10.1126/science.1253525.
Gagnon, M. G., Lin, J., Bulkley, D., and Steitz, T. A. Fri . "Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome". United States. doi:10.1126/science.1253525.
@article{osti_1354313,
title = {Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome},
author = {Gagnon, M. G. and Lin, J. and Bulkley, D. and Steitz, T. A.},
abstractNote = {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.},
doi = {10.1126/science.1253525},
journal = {Science},
issn = {0036-8075},
number = 6197,
volume = 345,
place = {United States},
year = {2014},
month = {8}
}