View source for 5imr


==Structure of ribosome bound to cofactor at 5.7 angstrom resolution==
<SX load='5imr' size='340' side='right' viewer='molstar' caption='[[5imr]], [[Resolution|resolution]] 5.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5imr]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IMR 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]] 5.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</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=5imr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5imr OCA], [https://pdbe.org/5imr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5imr RCSB], [https://www.ebi.ac.uk/pdbsum/5imr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5imr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RS2_THET8 RS2_THET8] Spans the head-body hinge region of the 30S subunit. Is loosely associated with the 30S subunit.[HAMAP-Rule:MF_00291_B]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Elongation factor 4 (EF4) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors, along with elongation factor G (EF-G) and BPI-inducible protein A (BipA). Although EF4 is highly conserved in bacterial, mitochondrial, and chloroplast genomes, its exact biological function remains controversial. Here, we present the cryo-EM reconstitution of the GTP form of EF4 bound to the ribosome with P- and E-site tRNAs at 3.8 A resolution. Interestingly, our structure reveals an unrotated ribosome rather than a clockwise-rotated ribosome, as observed in the presence of EF4-GDP and P-site tRNA. In addition, we also observed an counterclockwise rotated form of the above complex at 5.7 A resolution. Taken together, our results shed light on the interactions formed between EF4, the ribosome, and the P-site tRNA and illuminate the GTPase activation mechanism at previously unresolved detail.

Structure of the GTP form of elongation factor 4 (EF4) bound to the ribosome.,Kumar V, Ero R, Ahmed T, Goh KJ, Zhan Y, Bhushan S, Gao YG J Biol Chem. 2016 May 2. pii: jbc.M116.725945. PMID:27137929<ref>PMID:27137929</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5imr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
*[[Ribosomal protein THX 3D structures|Ribosomal protein THX 3D structures]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Ahmed T]]
[[Category: Bhushan S]]
[[Category: Ero R]]
[[Category: Gao YG]]
[[Category: Jian GK]]
[[Category: Kumar V]]
[[Category: Zhan Y]]