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| | <SX load='4d67' size='340' side='right' viewer='molstar' caption='[[4d67]], [[Resolution|resolution]] 9.00Å' scene=''> | | <SX load='4d67' size='340' side='right' viewer='molstar' caption='[[4d67]], [[Resolution|resolution]] 9.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d67]] is a 46 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D67 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4D67 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d67]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D67 FirstGlance]. <br> |
| - | </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=4d67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d67 OCA], [http://pdbe.org/4d67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d67 RCSB], [http://www.ebi.ac.uk/pdbsum/4d67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d67 ProSAT]</span></td></tr> | + | </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=4d67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d67 OCA], [https://pdbe.org/4d67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d67 RCSB], [https://www.ebi.ac.uk/pdbsum/4d67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d67 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Hilal, T]] | + | [[Category: Hilal T]] |
| - | [[Category: Mielke, T]] | + | [[Category: Mielke T]] |
| - | [[Category: Muhs, M]] | + | [[Category: Muhs M]] |
| - | [[Category: Pestova, T V]] | + | [[Category: Pestova TV]] |
| - | [[Category: Sanbonmatsu, K Y]] | + | [[Category: Sanbonmatsu KY]] |
| - | [[Category: Skabkin, M A]] | + | [[Category: Skabkin MA]] |
| - | [[Category: Spahn, C M.T]] | + | [[Category: Spahn CMT]] |
| - | [[Category: Crpv ire]]
| + | |
| - | [[Category: Release factor]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Termination]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The cricket paralysis virus (CrPV) uses an internal ribosomal entry site (IRES) to hijack the ribosome. In a remarkable RNA-based mechanism involving neither initiation factor nor initiator tRNA, the CrPV IRES jumpstarts translation in the elongation phase from the ribosomal A site. Here, we present cryoelectron microscopy (cryo-EM) maps of 80SCrPV-STOPeRF1eRF3GMPPNP and 80SCrPV-STOPeRF1 complexes, revealing a previously unseen binding state of the IRES and directly rationalizing that an eEF2-dependent translocation of the IRES is required to allow the first A-site occupation. During this unusual translocation event, the IRES undergoes a pronounced conformational change to a more stretched conformation. At the same time, our structural analysis provides information about the binding modes of eRF1eRF3GMPPNP and eRF1 in a minimal system. It shows that neither eRF3 nor ABCE1 are required for the active conformation of eRF1 at the intersection between eukaryotic termination and recycling.
Cryo-EM of Ribosomal 80S Complexes with Termination Factors Reveals the Translocated Cricket Paralysis Virus IRES.,Muhs M, Hilal T, Mielke T, Skabkin MA, Sanbonmatsu KY, Pestova TV, Spahn CM Mol Cell. 2015 Feb 5;57(3):422-432. doi: 10.1016/j.molcel.2014.12.016. Epub 2015 , Jan 15. PMID:25601755[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Muhs M, Hilal T, Mielke T, Skabkin MA, Sanbonmatsu KY, Pestova TV, Spahn CM. Cryo-EM of Ribosomal 80S Complexes with Termination Factors Reveals the Translocated Cricket Paralysis Virus IRES. Mol Cell. 2015 Feb 5;57(3):422-432. doi: 10.1016/j.molcel.2014.12.016. Epub 2015 , Jan 15. PMID:25601755 doi:http://dx.doi.org/10.1016/j.molcel.2014.12.016
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