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Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation

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Agrawal, Rajendra K., Penczek, Pawel, Grassucci, Robert A., Frank, Joachim·1998·Proceedings of the National Academy of Sciences

Abstract

During protein synthesis, elongation factor G (EF-G) binds to the ribosome and promotes the step of translocation, a process in which tRNA moves from the A to the P site of the ribosome and the mRNA is advanced by one codon. By using three-dimensional cryo-electron microscopy, we have visualized EF-G in a ribosome–EF-G–GDP–fusidic acid complex. Fitting the crystal structure of EF-G–GDP into the cryo density map reveals a large conformational change mainly associated with domain IV, the domain that mimics the shape of the anticodon arm of the tRNA in the structurally homologous ternary complex of Phe-tRNA Phe , EF-Tu, and a GTP analog. The tip portion of this domain is found in a position that overlaps the anticodon arm of the A-site tRNA, whose position in the ribosome is known from a study of the pretranslocational complex, implying that EF-G displaces the A-site tRNA to the P site by physical interaction with the anticodon arm.

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Metadata

Authors
Agrawal, R. K., Penczek, P., Grassucci, R. A., & Frank, J.
Venue
Proceedings of the National Academy of Sciences
Published
1998-05-26
Volume
95
Issue
11
Pages
6134-6138
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2152348402
Cited by
325
References
0
FWCI
11.59
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation. https://app.cochat.ai/papers/10.1073/pnas.95.11.6134
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Agrawal, R. K., Penczek, P., Grassucci, R. A., & Frank, J. (1998). Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.11.6134

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