View source for 6enu


==Polyproline-stalled ribosome in the presence of elongation-factor P (EF-P)==
<SX load='6enu' size='340' side='right' viewer='molstar' caption='[[6enu]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6enu]] 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=6ENU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ENU 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]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KEO:(2~{S},4~{S})-2-azanyl-6-[[(3~{S})-3,6-bis(azanyl)hexanoyl]amino]-4-oxidanyl-hexanoic+acid'>KEO</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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=6enu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6enu OCA], [https://pdbe.org/6enu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6enu RCSB], [https://www.ebi.ac.uk/pdbsum/6enu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6enu ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/RL18_ECOLI RL18_ECOLI] This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.<ref>PMID:353728</ref> 
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== Publication Abstract from PubMed ==
Ribosomes synthesizing proteins containing consecutive proline residues become stalled and require rescue via the action of uniquely modified translation elongation factors, EF-P in bacteria, or archaeal/eukaryotic a/eIF5A. To date, no structures exist of EF-P or eIF5A in complex with translating ribosomes stalled at polyproline stretches, and thus structural insight into how EF-P/eIF5A rescue these arrested ribosomes has been lacking. Here we present cryo-EM structures of ribosomes stalled on proline stretches, without and with modified EF-P. The structures suggest that the favored conformation of the polyproline-containing nascent chain is incompatible with the peptide exit tunnel of the ribosome and leads to destabilization of the peptidyl-tRNA. Binding of EF-P stabilizes the P-site tRNA, particularly via interactions between its modification and the CCA end, thereby enforcing an alternative conformation of the polyproline-containing nascent chain, which allows a favorable substrate geometry for peptide bond formation.

Structural Basis for Polyproline-Mediated Ribosome Stalling and Rescue by the Translation Elongation Factor EF-P.,Huter P, Arenz S, Bock LV, Graf M, Frister JO, Heuer A, Peil L, Starosta AL, Wohlgemuth I, Peske F, Novacek J, Berninghausen O, Grubmuller H, Tenson T, Beckmann R, Rodnina MV, Vaiana AC, Wilson DN Mol Cell. 2017 Nov 2;68(3):515-527.e6. doi: 10.1016/j.molcel.2017.10.014. PMID:29100052<ref>PMID:29100052</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
*[[Ribosome 3D structures|Ribosome 3D structures]]
== References ==
<references/>
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Arenz S]]
[[Category: Huter P]]
[[Category: Wilson DN]]