3j15

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[[Image:3j15.png|left|200px]]
 
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==Model of ribosome-bound archaeal Pelota and ABCE1==
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The line below this paragraph, containing "STRUCTURE_3j15", creates the "Structure Box" on the page.
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<SX load='3j15' size='340' side='right' viewer='molstar' caption='[[3j15]], [[Resolution|resolution]] 6.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3j15]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] and [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J15 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 6.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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{{STRUCTURE_3j15| PDB=3j15 | SCENE= }}
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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=3j15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j15 OCA], [https://pdbe.org/3j15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j15 RCSB], [https://www.ebi.ac.uk/pdbsum/3j15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j15 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PELO_THEKO PELO_THEKO] May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ribosome-driven protein biosynthesis is comprised of four phases: initiation, elongation, termination and recycling. In bacteria, ribosome recycling requires ribosome recycling factor and elongation factor G, and several structures of bacterial recycling complexes have been determined. In the eukaryotic and archaeal kingdoms, however, recycling involves the ABC-type ATPase ABCE1 and little is known about its structural basis. Here we present cryo-electron microscopy reconstructions of eukaryotic and archaeal ribosome recycling complexes containing ABCE1 and the termination factor paralogue Pelota. These structures reveal the overall binding mode of ABCE1 to be similar to canonical translation factors. Moreover, the iron-sulphur cluster domain of ABCE1 interacts with and stabilizes Pelota in a conformation that reaches towards the peptidyl transferase centre, thus explaining how ABCE1 may stimulate peptide-release activity of canonical termination factors. Using the mechanochemical properties of ABCE1, a conserved mechanism in archaea and eukaryotes is suggested that couples translation termination to recycling, and eventually to re-initiation.
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===Model of ribosome-bound archaeal Pelota and ABCE1===
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Structural basis of highly conserved ribosome recycling in eukaryotes and archaea.,Becker T, Franckenberg S, Wickles S, Shoemaker CJ, Anger AM, Armache JP, Sieber H, Ungewickell C, Berninghausen O, Daberkow I, Karcher A, Thomm M, Hopfner KP, Green R, Beckmann R Nature. 2012 Feb 22;482(7386):501-6. doi: 10.1038/nature10829. PMID:22358840<ref>PMID:22358840</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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The line below this paragraph, {{ABSTRACT_PUBMED_22358840}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3j15" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 22358840 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22358840}}
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__TOC__
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</SX>
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==About this Structure==
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[[Category: Large Structures]]
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[[3j15]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J15 OCA].
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==Reference==
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<ref group="xtra">PMID:022358840</ref><references group="xtra"/>
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[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
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[[Category: Anger, A M.]]
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[[Category: Thermococcus kodakarensis]]
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[[Category: Armache, J P.]]
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[[Category: Anger AM]]
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[[Category: Becker, T.]]
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[[Category: Armache J-P]]
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[[Category: Beckmann, R.]]
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[[Category: Becker T]]
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[[Category: Berninghausen, O.]]
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[[Category: Beckmann R]]
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[[Category: Daberkow, I.]]
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[[Category: Berninghausen O]]
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[[Category: Franckenberg, S.]]
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[[Category: Daberkow I]]
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[[Category: Green, R.]]
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[[Category: Franckenberg S]]
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[[Category: Hopfner, K P.]]
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[[Category: Green R]]
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[[Category: Karcher, A.]]
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[[Category: Hopfner K-P]]
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[[Category: Shoemaker, C J.]]
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[[Category: Karcher A]]
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[[Category: Sieber, H.]]
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[[Category: Shoemaker CJ]]
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[[Category: Thomm, M.]]
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[[Category: Sieber H]]
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[[Category: Ungewickell, C.]]
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[[Category: Thomm M]]
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[[Category: Wickles, S.]]
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[[Category: Ungewickell C]]
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[[Category: Archaea]]
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[[Category: Wickles S]]
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[[Category: Ribosome]]
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[[Category: Ribosome recycling]]
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[[Category: Translation-transport protein complex]]
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Current revision

Model of ribosome-bound archaeal Pelota and ABCE1

3j15, resolution 6.60Å

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OCA

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