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Title: Crystal Structures of EF-G-Ribosome Complexes Trapped in Intermediate States of Translocation

Abstract

Translocation of messenger and transfer RNA (mRNA and tRNA) through the ribosome is a crucial step in protein synthesis, whose mechanism is not yet understood. The crystal structures of three Thermus ribosome-tRNA-mRNA–EF-G complexes trapped with β,γ-imidoguanosine 5'-triphosphate (GDPNP) or fusidic acid reveal conformational changes occurring during intermediate states of translocation, including large-scale rotation of the 30S subunit head and body. In all complexes, the tRNA acceptor ends occupy the 50S subunit E site, while their anticodon stem loops move with the head of the 30S subunit to positions between the P and E sites, forming chimeric intermediate states. Two universally conserved bases of 16S ribosomal RNA that intercalate between bases of the mRNA may act as “pawls” of a translocational ratchet. These findings provide new insights into the molecular mechanism of ribosomal translocation.

Authors:
; ; ;  [1]
  1. UCSC
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1097291
Resource Type:
Journal Article
Journal Name:
Science
Additional Journal Information:
Journal Volume: 340; Journal Issue: 06, 2013; Journal ID: ISSN 0036-8075
Publisher:
AAAS
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Zhou, Jie, Lancaster, Laura, Donohue, John Paul, and Noller, Harry F. Crystal Structures of EF-G-Ribosome Complexes Trapped in Intermediate States of Translocation. United States: N. p., 2013. Web. doi:10.1126/science.1236086.
Zhou, Jie, Lancaster, Laura, Donohue, John Paul, & Noller, Harry F. Crystal Structures of EF-G-Ribosome Complexes Trapped in Intermediate States of Translocation. United States. doi:10.1126/science.1236086.
Zhou, Jie, Lancaster, Laura, Donohue, John Paul, and Noller, Harry F. Tue . "Crystal Structures of EF-G-Ribosome Complexes Trapped in Intermediate States of Translocation". United States. doi:10.1126/science.1236086.
@article{osti_1097291,
title = {Crystal Structures of EF-G-Ribosome Complexes Trapped in Intermediate States of Translocation},
author = {Zhou, Jie and Lancaster, Laura and Donohue, John Paul and Noller, Harry F.},
abstractNote = {Translocation of messenger and transfer RNA (mRNA and tRNA) through the ribosome is a crucial step in protein synthesis, whose mechanism is not yet understood. The crystal structures of three Thermus ribosome-tRNA-mRNA–EF-G complexes trapped with β,γ-imidoguanosine 5'-triphosphate (GDPNP) or fusidic acid reveal conformational changes occurring during intermediate states of translocation, including large-scale rotation of the 30S subunit head and body. In all complexes, the tRNA acceptor ends occupy the 50S subunit E site, while their anticodon stem loops move with the head of the 30S subunit to positions between the P and E sites, forming chimeric intermediate states. Two universally conserved bases of 16S ribosomal RNA that intercalate between bases of the mRNA may act as “pawls” of a translocational ratchet. These findings provide new insights into the molecular mechanism of ribosomal translocation.},
doi = {10.1126/science.1236086},
journal = {Science},
issn = {0036-8075},
number = 06, 2013,
volume = 340,
place = {United States},
year = {2013},
month = {11}
}