3j0d

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==Models for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex==
==Models for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex==
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<StructureSection load='3j0d' size='340' side='right' caption='[[3j0d]], [[Resolution|resolution]] 11.10&Aring;' scene=''>
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<SX load='3j0d' size='340' side='right' viewer='molstar' caption='[[3j0d]], [[Resolution|resolution]] 11.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3j0d]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J0D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J0D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3j0d]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J0D FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j0d RCSB], [http://www.ebi.ac.uk/pdbsum/3j0d PDBsum]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 11.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0d OCA], [https://pdbe.org/3j0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j0d RCSB], [https://www.ebi.ac.uk/pdbsum/3j0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j0d ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B]
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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.
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Structural insights into initial and intermediate steps of the ribosome-recycling process.,Yokoyama T, Shaikh TR, Iwakura N, Kaji H, Kaji A, Agrawal RK EMBO J. 2012 Mar 2;31(7):1836-46. doi: 10.1038/emboj.2012.22. PMID:22388519<ref>PMID:22388519</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Ribosomal protein L11 3D structures|Ribosomal protein L11 3D structures]]
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*[[Ribosomal protein S12|Ribosomal protein S12]]
*[[Ribosome 3D structures|Ribosome 3D structures]]
*[[Ribosome 3D structures|Ribosome 3D structures]]
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== References ==
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*[[Ribosome recycling factor|Ribosome recycling factor]]
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<references/>
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__TOC__
__TOC__
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</StructureSection>
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</SX>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Thermus thermophilus]]
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[[Category: Large Structures]]
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[[Category: Agrawal, R K]]
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[[Category: Agrawal RK]]
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[[Category: Iwakura, N]]
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[[Category: Iwakura N]]
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[[Category: Kaji, A]]
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[[Category: Kaji A]]
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[[Category: Kaji, H]]
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[[Category: Kaji H]]
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[[Category: Shaikh, T R]]
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[[Category: Shaikh TR]]
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[[Category: Yokoyama, T]]
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[[Category: Yokoyama T]]
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[[Category: Ribosome]]
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[[Category: Ribosome recycling factor]]
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[[Category: Translation]]
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Current revision

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

3j0d, resolution 11.10Å

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