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| | <SX load='5lw7' size='340' side='right' viewer='molstar' caption='[[5lw7]], [[Resolution|resolution]] 17.00Å' scene=''> | | <SX load='5lw7' size='340' side='right' viewer='molstar' caption='[[5lw7]], [[Resolution|resolution]] 17.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lw7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrab Pyrab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LW7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LW7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lw7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi_GE5 Pyrococcus abyssi GE5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LW7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 17Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v6u|4v6u]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAB0824 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272844 PYRAB])</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=5lw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lw7 OCA], [https://pdbe.org/5lw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lw7 RCSB], [https://www.ebi.ac.uk/pdbsum/5lw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lw7 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lw7 OCA], [http://pdbe.org/5lw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lw7 RCSB], [http://www.ebi.ac.uk/pdbsum/5lw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lw7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9UZA4_PYRAB Q9UZA4_PYRAB] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pyrab]] | + | [[Category: Pyrococcus abyssi GE5]] |
| - | [[Category: Beckmann, R]] | + | [[Category: Beckmann R]] |
| - | [[Category: Gerovac, M]] | + | [[Category: Gerovac M]] |
| - | [[Category: Heuer, A]] | + | [[Category: Heuer A]] |
| - | [[Category: Tampe, R]] | + | [[Category: Tampe R]] |
| - | [[Category: Abce1]]
| + | |
| - | [[Category: Recycling]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| Structural highlights
Function
Q9UZA4_PYRAB
Publication Abstract from PubMed
Ribosome recycling orchestrated by the ATP binding cassette (ABC) protein ABCE1 can be considered as the final-or the first-step within the cyclic process of protein synthesis, connecting translation termination and mRNA surveillance with re-initiation. An ATP-dependent tweezer-like motion of the nucleotide-binding domains in ABCE1 transfers mechanical energy to the ribosome and tears the ribosome subunits apart. The post-recycling complex (PRC) then re-initiates mRNA translation. Here, we probed the so far unknown architecture of the 1-MDa PRC (40S/30S.ABCE1) by chemical cross-linking and mass spectrometry (XL-MS). Our study reveals ABCE1 bound to the translational factor-binding (GTPase) site with multiple cross-link contacts of the helix-loop-helix motif to the S24e ribosomal protein. Cross-linking of the FeS cluster domain to the ribosomal protein S12 substantiates an extreme lever-arm movement of the FeS cluster domain during ribosome recycling. We were thus able to reconstitute and structurally analyse a key complex in the translational cycle, resembling the link between translation initiation and ribosome recycling.
Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry.,Kiosze-Becker K, Ori A, Gerovac M, Heuer A, Nurenberg-Goloub E, Rashid UJ, Becker T, Beckmann R, Beck M, Tampe R Nat Commun. 2016 Nov 8;7:13248. doi: 10.1038/ncomms13248. PMID:27824037[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kiosze-Becker K, Ori A, Gerovac M, Heuer A, Nurenberg-Goloub E, Rashid UJ, Becker T, Beckmann R, Beck M, Tampe R. Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry. Nat Commun. 2016 Nov 8;7:13248. doi: 10.1038/ncomms13248. PMID:27824037 doi:http://dx.doi.org/10.1038/ncomms13248
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