6y2l: Difference between revisions

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-'''Unreleased structure'''
-The entry 6y2l is ON HOLD  until Paper Publication
+==Structure of human ribosome in POST state==
+<StructureSection load='6y2l' size='340' side='right'caption='[[6y2l]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6y2l]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y2L 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]] 3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3HE:4-{(2R)-2-[(1S,3S,5S)-3,5-DIMETHYL-2-OXOCYCLOHEXYL]-2-HYDROXYETHYL}PIPERIDINE-2,6-DIONE'>3HE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6y2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y2l OCA], [https://pdbe.org/6y2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y2l RCSB], [https://www.ebi.ac.uk/pdbsum/6y2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y2l ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RL9_HUMAN RL9_HUMAN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Ribosomes undergo multiple conformational transitions during translation elongation. Here, we report the high-resolution cryoelectron microscopy (cryo-EM) structure of the human 80S ribosome in the post-decoding pre-translocation state (classical-PRE) at 3.3-A resolution along with the rotated (hybrid-PRE) and the post-translocation states (POST). The classical-PRE state ribosome structure reveals a previously unobserved interaction between the C-terminal region of the conserved ribosomal protein uS19 and the A- and P-site tRNAs and the mRNA in the decoding site. In addition to changes in the inter-subunit bridges, analysis of different ribosomal conformations reveals the dynamic nature of this domain and suggests a role in tRNA accommodation and translocation during elongation. Furthermore, we show that disease-associated mutations in uS19 result in increased frameshifting. Together, this structure-function analysis provides mechanistic insights into the role of the uS19 C-terminal tail in the context of mammalian ribosomes.
-Authors:
+Dynamics of uS19 C-Terminal Tail during the Translation Elongation Cycle in Human Ribosomes.,Bhaskar V, Graff-Meyer A, Schenk AD, Cavadini S, von Loeffelholz O, Natchiar SK, Artus-Revel CG, Hotz HR, Bretones G, Klaholz BP, Chao JA Cell Rep. 2020 Apr 7;31(1):107473. doi: 10.1016/j.celrep.2020.03.037. PMID:32268098<ref>PMID:32268098</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6y2l" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ribosome 3D structures|Ribosome 3D structures]]
+*[[3D sructureseceptor for activated protein kinase C 1|3D sructureseceptor for activated protein kinase C 1]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Bhaskar V]]
+[[Category: Cavadini S]]
+[[Category: Chao JA]]
+[[Category: Klaholz BP]]
+[[Category: Natchiar SK]]
+[[Category: Schenk AD]]
+[[Category: Von Loeffelholz O]]