PMID:15616575
| Citation |
Wilson, DN, Schluenzen, F, Harms, JM, Yoshida, T, Ohkubo, T, Albrecht, R, Buerger, J, Kobayashi, Y and Fucini, P (2005) X-ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit. EMBO J. 24:251-60 |
|---|---|
| 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. |
| Links |
PubMed PMC545814 Online version:10.1038/sj.emboj.7600525 |
| Keywords |
Amino Acid Sequence; Cryoelectron Microscopy; Crystallography, X-Ray; Deinococcus/metabolism; Escherichia coli/metabolism; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Proteins/metabolism; Ribosomal Proteins; Ribosomes/metabolism; Sequence Homology, Amino Acid |
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