3j15
From Proteopedia
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- | [[ | + | ==Model of ribosome-bound archaeal Pelota and ABCE1== |
+ | <StructureSection load='3j15' size='340' side='right' caption='[[3j15]], [[Resolution|resolution]] 6.60Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[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]. 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> | ||
+ | </td></tr><tr><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><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j16|3j16]]</td></tr> | ||
+ | <tr><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://www.rcsb.org/pdb/explore.do?structureId=3j15 RCSB], [http://www.ebi.ac.uk/pdbsum/3j15 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:22358840</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Anger, A M.]] | [[Category: Anger, A M.]] |
Revision as of 09:39, 21 May 2014
Model of ribosome-bound archaeal Pelota and ABCE1
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Categories: Pyrococcus furiosus | Anger, A M. | Armache, J P. | Becker, T. | Beckmann, R. | Berninghausen, O. | Daberkow, I. | Franckenberg, S. | Green, R. | Hopfner, K P. | Karcher, A. | Shoemaker, C J. | Sieber, H. | Thomm, M. | Ungewickell, C. | Wickles, S. | Archaea | Ribosome | Ribosome recycling | Translation-transport protein complex