1Y69

RRF domain I in complex with the 50S ribosomal subunit from Deinococcus radiodurans

Summary for 1Y69

• Entry DOI: 10.2210/pdb1y69/pdb
• Related: 1EK8 1NKW
• Descriptor: 23S ribosomal RNA, 5S ribosomal RNA, 50S ribosomal protein L16, ... (5 entities in total)
• Functional Keywords: ribosome, 50s, rrf, recycling factor
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A805
• Total number of polymer chains: 5
• Total formula weight: 1011896.56

Authors

Wilson, D.N.,Schluenzen, F.,Harms, J.M.,Yoshida, T.,Ohkubo, T.,Albrecht, R.,Buerger, J.,Kobayashi, Y.,Fucini, P. (deposition date: 2004-12-04, release date: 2005-03-01, Last modification date: 2023-08-23)

Primary citation

Wilson, D.N.,Schluenzen, F.,Harms, J.M.,Yoshida, T.,Ohkubo, T.,Albrecht, R.,Buerger, J.,Kobayashi, Y.,Fucini, P.
X-ray crystallography on ribosome recycling: mechanism of binding and action of RRF on the 50S ribosomal subunit
EMBO J., 24:251-260, 2005

PubMed Abstract: This study presents the crystal structure of domain I of the Escherichia coli ribosome recycling factor (RRF) bound to the Deinococcus radiodurans 50S subunit. The orientation of RRF is consistent with the position determined on a 70S-RRF complex by cryoelectron microscopy (cryo-EM). Alignment, however, requires a rotation of 7 degrees and a shift of the cryo-EM RRF by a complete turn of an alpha-helix, redefining the contacts established with ribosomal components. At 3.3 A resolution, RRF is seen to interact exclusively with ribosomal elements associated with tRNA binding and/or translocation. Furthermore, these results now provide a high-resolution structural description of the conformational changes that were suspected to occur on the 70S-RRF complex, which has implications for the synergistic action of RRF with elongation factor G (EF-G). Specifically, the tip of the universal bridge element H69 is shifted by 20 A toward h44 of the 30S subunit, suggesting that RRF primes the intersubunit bridge B2a for the action of EF-G. Collectively, our data enable a model to be proposed for the dual action of EF-G and RRF during ribosome recycling.

PubMed: 15616575
DOI: 10.1038/sj.emboj.7600525

Experimental method

X-RAY DIFFRACTION (3.33 Å)