1y69
From Proteopedia
(New page: 200px<br /><applet load="1y69" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y69, resolution 3.33Å" /> '''RRF domain I in comp...) |
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| - | [[Image:1y69.gif|left|200px]]<br /><applet load="1y69" size=" | + | [[Image:1y69.gif|left|200px]]<br /><applet load="1y69" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y69, resolution 3.33Å" /> | caption="1y69, resolution 3.33Å" /> | ||
'''RRF domain I in complex with the 50S ribosomal subunit from Deinococcus radiodurans'''<br /> | '''RRF domain I in complex with the 50S ribosomal subunit from Deinococcus radiodurans'''<br /> | ||
==Overview== | ==Overview== | ||
| - | This study presents the crystal structure of domain I of the Escherichia | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y69 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http:// | + | 1Y69 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y69 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Buerger, J.]] | [[Category: Buerger, J.]] | ||
[[Category: Fucini, P.]] | [[Category: Fucini, P.]] | ||
| - | [[Category: Harms, J | + | [[Category: Harms, J M.]] |
[[Category: Kobayashi, Y.]] | [[Category: Kobayashi, Y.]] | ||
[[Category: Ohkubo, T.]] | [[Category: Ohkubo, T.]] | ||
[[Category: Schluenzen, F.]] | [[Category: Schluenzen, F.]] | ||
| - | [[Category: Wilson, D | + | [[Category: Wilson, D N.]] |
[[Category: Yoshida, T.]] | [[Category: Yoshida, T.]] | ||
[[Category: 50s]] | [[Category: 50s]] | ||
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[[Category: rrf]] | [[Category: rrf]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:02:10 2008'' |
Revision as of 14:02, 21 February 2008
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RRF domain I in complex with the 50S ribosomal subunit from Deinococcus radiodurans
Overview
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.
About this Structure
1Y69 is a Protein complex structure of sequences from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
X-ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit., Wilson DN, Schluenzen F, Harms JM, Yoshida T, Ohkubo T, Albrecht R, Buerger J, Kobayashi Y, Fucini P, EMBO J. 2005 Jan 26;24(2):251-60. Epub 2004 Dec 23. PMID:15616575
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