3J0E

Models for the T. thermophilus ribosome recycling factor and the E. coli elongation factor G bound to the E. coli post-termination complex

Summary for 3J0E

• Entry DOI: 10.2210/pdb3j0e/pdb
• EMDB information: 1917 1918
• Descriptor: ribosomal 23S RNA, ribosomal 16S RNA, 30S ribosomal protein S12, ... (9 entities in total)
• Functional Keywords: ribosome, ribosome recycling factor, elongation factor g, translation
• Biological source: Escherichia coli; More
• Total number of polymer chains: 9
• Total formula weight: 146842.86

Authors

Yokoyama, T.,Shaikh, T.R.,Iwakura, N.,Kaji, H.,Kaji, A.,Agrawal, R.K. (deposition date: 2011-06-29, release date: 2012-04-25, Last modification date: 2024-02-21)

Primary citation

Yokoyama, T.,Shaikh, T.R.,Iwakura, N.,Kaji, H.,Kaji, A.,Agrawal, R.K.
Structural insights into initial and intermediate steps of the ribosome-recycling process.
Embo J., 31:1836-1846, 2012

PubMed Abstract: The ribosome-recycling factor (RRF) and elongation factor-G (EF-G) disassemble the 70S post-termination complex (PoTC) into mRNA, tRNA, and two ribosomal subunits. We have determined cryo-electron microscopic structures of the PoTC·RRF complex, with and without EF-G. We find that domain II of RRF initially interacts with universally conserved residues of the 23S rRNA helices 43 and 95, and protein L11 within the 50S ribosomal subunit. Upon EF-G binding, both RRF and tRNA are driven towards the tRNA-exit (E) site, with a large rotational movement of domain II of RRF towards the 30S ribosomal subunit. During this intermediate step of the recycling process, domain II of RRF and domain IV of EF-G adopt hitherto unknown conformations. Furthermore, binding of EF-G to the PoTC·RRF complex reverts the ribosome from ratcheted to unratcheted state. These results suggest that (i) the ribosomal intersubunit reorganizations upon RRF binding and subsequent EF-G binding could be instrumental in destabilizing the PoTC and (ii) the modes of action of EF-G during tRNA translocation and ribosome-recycling steps are markedly different.

PubMed: 22388519
DOI: 10.1038/emboj.2012.22

Experimental method

ELECTRON MICROSCOPY (9.9 Å)