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| | ==Model of ribosome-bound archaeal Pelota and ABCE1== | | ==Model of ribosome-bound archaeal Pelota and ABCE1== |
| - | <StructureSection load='3j15' size='340' side='right' caption='[[3j15]], [[Resolution|resolution]] 6.60Å' scene=''> | + | <SX load='3j15' size='340' side='right' viewer='molstar' caption='[[3j15]], [[Resolution|resolution]] 6.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3j15]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J15 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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]] 6.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j16|3j16]]</td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pelA, TK0964 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</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=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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j15 OCA], [http://pdbe.org/3j15 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j15 RCSB], [http://www.ebi.ac.uk/pdbsum/3j15 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j15 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). | + | [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). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Atcc 43587]] | + | [[Category: Large Structures]] |
| - | [[Category: Anger, A M]] | + | [[Category: Pyrococcus furiosus]] |
| - | [[Category: Armache, J P]] | + | [[Category: Thermococcus kodakarensis]] |
| - | [[Category: Becker, T]] | + | [[Category: Anger AM]] |
| - | [[Category: Beckmann, R]] | + | [[Category: Armache J-P]] |
| - | [[Category: Berninghausen, O]] | + | [[Category: Becker T]] |
| - | [[Category: Daberkow, I]] | + | [[Category: Beckmann R]] |
| - | [[Category: Franckenberg, S]] | + | [[Category: Berninghausen O]] |
| - | [[Category: Green, R]] | + | [[Category: Daberkow I]] |
| - | [[Category: Hopfner, K P]] | + | [[Category: Franckenberg S]] |
| - | [[Category: Karcher, A]] | + | [[Category: Green R]] |
| - | [[Category: Shoemaker, C J]] | + | [[Category: Hopfner K-P]] |
| - | [[Category: Sieber, H]] | + | [[Category: Karcher A]] |
| - | [[Category: Thomm, M]] | + | [[Category: Shoemaker CJ]] |
| - | [[Category: Ungewickell, C]] | + | [[Category: Sieber H]] |
| - | [[Category: Wickles, S]] | + | [[Category: Thomm M]] |
| - | [[Category: Archaea]]
| + | [[Category: Ungewickell C]] |
| - | [[Category: Ribosome]]
| + | [[Category: Wickles S]] |
| - | [[Category: Ribosome recycling]]
| + | |
| - | [[Category: Translation-transport protein complex]]
| + | |
| Structural highlights
Function
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).
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. Structural basis of highly conserved ribosome recycling in eukaryotes and archaea. Nature. 2012 Feb 22;482(7386):501-6. doi: 10.1038/nature10829. PMID:22358840 doi:10.1038/nature10829
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