View source for 3jce


==Structure of Escherichia coli EF4 in pretranslocational ribosomes (Pre EF4)==
<SX load='3jce' size='340' side='right' viewer='molstar' caption='[[3jce]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3jce]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JCE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jce OCA], [https://pdbe.org/3jce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jce RCSB], [https://www.ebi.ac.uk/pdbsum/3jce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jce ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL36_ECOLI RL36_ECOLI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
EF4 catalyzes tRNA back-translocation through an unknown mechanism. We report cryo-EM structures of Escherichia coli EF4 in post- and pretranslocational ribosomes (Post- and Pre-EF4) at 3.7- and 3.2-A resolution, respectively. In Post-EF4, peptidyl-tRNA occupies the peptidyl (P) site, but the interaction between its CCA end and the P loop is disrupted. In Pre-EF4, the peptidyl-tRNA assumes a unique position near the aminoacyl (A) site, denoted the A site/EF4 bound (A/4) site, with a large displacement at its acceptor arm. Mutagenesis analyses suggest that a specific region in the EF4 C-terminal domain (CTD) interferes with base-pairing between the peptidyl-tRNA 3'-CCA and the P loop, whereas the EF4 CTD enhances peptidyl-tRNA interaction at the A/4 site. Therefore, EF4 induces back-translocation by disengaging the tRNA's CCA end from the peptidyl transferase center of the translating ribosome.

EF4 disengages the peptidyl-tRNA CCA end and facilitates back-translocation on the 70S ribosome.,Zhang D, Yan K, Liu G, Song G, Luo J, Shi Y, Cheng E, Wu S, Jiang T, Lou J, Gao N, Qin Y Nat Struct Mol Biol. 2016 Feb;23(2):125-31. doi: 10.1038/nsmb.3160. Epub 2016 Jan, 25. PMID:26809121<ref>PMID:26809121</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3jce" style="background-color:#fffaf0;"></div>

==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
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</SX>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Cheng E]]
[[Category: Gao N]]
[[Category: Jiang T]]
[[Category: Liu G]]
[[Category: Low J]]
[[Category: Luo J]]
[[Category: Qin Y]]
[[Category: Shi Y]]
[[Category: Song G]]
[[Category: Wu S]]
[[Category: Yan K]]
[[Category: Zhang D]]