3j0e: Difference between revisions

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 ==Models for the T. thermophilus ribosome recycling factor and the E. coli elongation factor G bound to the E. coli post-termination complex==
-<StructureSection load='3j0e' size='340' side='right' caption='[[3j0e]], [[Resolution|resolution]] 9.90&Aring;' scene=''>
+<SX load='3j0e' size='340' side='right' viewer='molstar' caption='[[3j0e]], [[Resolution|resolution]] 9.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3j0e]] is a 9 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=3J0E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J0E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3j0e]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J0E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J0E FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j0e RCSB], [http://www.ebi.ac.uk/pdbsum/3j0e PDBsum]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9.9&#8491;</td></tr>
-<table>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0e OCA], [https://pdbe.org/3j0e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j0e RCSB], [https://www.ebi.ac.uk/pdbsum/3j0e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j0e ProSAT]</span></td></tr>
-<div style="background-color:#fffaf0;">
+</table>
-== Publication Abstract from PubMed ==
+== Function ==
-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.
+[https://www.uniprot.org/uniprot/RS12_ECOLI RS12_ECOLI] With S4 and S5 plays an important role in translational accuracy.[HAMAP-Rule:MF_00403_B]  Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (By similarity).[HAMAP-Rule:MF_00403_B]  Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit.[HAMAP-Rule:MF_00403_B]
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[Elongation factor|Elongation factor]]
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
-== References ==
+*[[Ribosomal protein S12|Ribosomal protein S12]]
-<references/>
+*[[Ribosome recycling factor|Ribosome recycling factor]]
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Escherichia coli]]
+[[Category: Large Structures]]
 [[Category: Thermus thermophilus]]
-[[Category: Agrawal, R K.]]
+[[Category: Agrawal RK]]
-[[Category: Iwakura, N.]]
+[[Category: Iwakura N]]
-[[Category: Kaji, A.]]
+[[Category: Kaji A]]
-[[Category: Kaji, H.]]
+[[Category: Kaji H]]
-[[Category: Shaikh, T R.]]
+[[Category: Shaikh TR]]
-[[Category: Yokoyama, T.]]
+[[Category: Yokoyama T]]
-[[Category: Elongation factor g]]
-[[Category: Ribosome]]
-[[Category: Ribosome recycling factor]]
-[[Category: Translation]]