Structural mechanism of GTPase-powered ribosome-tRNA movement

Valentyn Petrychenko; Bee-Zen Peng; Ana C. de A. P. Schwarzer; Frank Peske; Marina V. Rodnina; Niels Fischer

doi:10.1038/s41467-021-26133-x

Nature Communications (Oct 2021)

Structural mechanism of GTPase-powered ribosome-tRNA movement

Valentyn Petrychenko,
Bee-Zen Peng,
Ana C. de A. P. Schwarzer,
Frank Peske,
Marina V. Rodnina,
Niels Fischer

Affiliations

Valentyn Petrychenko: Department of Structural Dynamics, Max Planck Institute for Biophysical Chemistry
Bee-Zen Peng: Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry
Ana C. de A. P. Schwarzer: Department of Structural Dynamics, Max Planck Institute for Biophysical Chemistry
Frank Peske: Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry
Marina V. Rodnina: Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry
Niels Fischer: Department of Structural Dynamics, Max Planck Institute for Biophysical Chemistry

DOI: https://doi.org/10.1038/s41467-021-26133-x
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 9

Abstract

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Movement of the ribosome along an mRNA requires the universally-conserved translocase (EF-G in bacteria) that couples GTP hydrolysis to directed movement. Here the authors use time-resolved Cryo-EM to visualize the GTPase-powered step on native translocating ribosomes and capture key translocation intermediates.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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