7PJX

Structure of the 70S-EF-G-GDP ribosome complex with tRNAs in hybrid state 1 (H1-EF-G-GDP)

This is a non-PDB format compatible entry.

Summary for 7PJX

• Entry DOI: 10.2210/pdb7pjx/pdb
• EMDB information: 13463
• Descriptor: 50S ribosomal protein L32, 50S ribosomal protein L2, 50S ribosomal protein L3, ... (61 entities in total)
• Functional Keywords: ef-g, robosome, 70s, apramycin, translocation, ribosome
• Biological source: Escherichia coli; More
• Total number of polymer chains: 59
• Total formula weight: 2311669.50

Authors

Petrychenko, V.,Peng, B.Z.,Schwarzer, A.C.,Peske, F.,Rodnina, M.V.,Fischer, N. (deposition date: 2021-08-24, release date: 2021-10-20, Last modification date: 2024-04-24)

Primary citation

Petrychenko, V.,Peng, B.Z.,de A P Schwarzer, A.C.,Peske, F.,Rodnina, M.V.,Fischer, N.
Structural mechanism of GTPase-powered ribosome-tRNA movement.
Nat Commun, 12:5933-5933, 2021

PubMed Abstract: GTPases are regulators of cell signaling acting as molecular switches. The translational GTPase EF-G stands out, as it uses GTP hydrolysis to generate force and promote the movement of the ribosome along the mRNA. The key unresolved question is how GTP hydrolysis drives molecular movement. Here, we visualize the GTPase-powered step of ongoing translocation by time-resolved cryo-EM. EF-G in the active GDP-Pi form stabilizes the rotated conformation of ribosomal subunits and induces twisting of the sarcin-ricin loop of the 23 S rRNA. Refolding of the GTPase switch regions upon Pi release initiates a large-scale rigid-body rotation of EF-G pivoting around the sarcin-ricin loop that facilitates back rotation of the ribosomal subunits and forward swiveling of the head domain of the small subunit, ultimately driving tRNA forward movement. The findings demonstrate how a GTPase orchestrates spontaneous thermal fluctuations of a large RNA-protein complex into force-generating molecular movement.

PubMed: 34635670
DOI: 10.1038/s41467-021-26133-x

Experimental method

ELECTRON MICROSCOPY (6.5 Å)