4d67: Difference between revisions

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-'''Unreleased structure'''
-The entry 4d67 is ON HOLD  until sometime in the future
+==Cryo-EM structures of ribosomal 80S complexes with termination factors and cricket paralysis virus IRES reveal the IRES in the translocated state==
+<SX load='4d67' size='340' side='right' viewer='molstar' caption='[[4d67]], [[Resolution|resolution]] 9.00&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9&#8491;</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>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Muhs, M., Hilal, T., Mielke, T., Skabkin, M.A., Sanbonmatsu, K.Y., Pestova, T.V., Spahn, C.M.T.
+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<ref>PMID:25601755</ref>
-Description: Cryo-EM structures of ribosomal 80S complexes with termination factors and cricket paralysis virus IRES reveal the IRES in the translocated state
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Sanbonmatsu, K.Y]]
+<div class="pdbe-citations 4d67" style="background-color:#fffaf0;"></div>
-[[Category: Skabkin, M.A]]
+== References ==
-[[Category: Muhs, M]]
+<references/>
-[[Category: Pestova, T.V]]
+__TOC__
-[[Category: Mielke, T]]
+</SX>
-[[Category: Hilal, T]]
+[[Category: Large Structures]]
-[[Category: Spahn, C.M.T]]
+[[Category: Oryctolagus cuniculus]]
+[[Category: Hilal T]]
+[[Category: Mielke T]]
+[[Category: Muhs M]]
+[[Category: Pestova TV]]
+[[Category: Sanbonmatsu KY]]
+[[Category: Skabkin MA]]
+[[Category: Spahn CMT]]