3j92: Difference between revisions
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{{Large structure}} | |||
==Structure and assembly pathway of the ribosome quality control complex== | ==Structure and assembly pathway of the ribosome quality control complex== | ||
<StructureSection load='3j92' size='340' side='right' caption='[[3j92]], [[Resolution|resolution]] 3.60Å' scene=''> | <StructureSection load='3j92' size='340' side='right' caption='[[3j92]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3j92]] is a 55 chain structure with sequence from [http://en.wikipedia.org/wiki/ ], [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J92 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3j92]] is a 55 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit], [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J92 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j92 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j92 RCSB], [http://www.ebi.ac.uk/pdbsum/3j92 PDBsum]</span></td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NEMF, SDCCAG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit]), LTN1, C21orf10, C21orf98, KIAA0714, RNF160, ZNF294, HSPC087 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j92 OCA], [http://pdbe.org/3j92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j92 RCSB], [http://www.ebi.ac.uk/pdbsum/3j92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j92 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
{{Large structure}} | {{Large structure}} | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3j92" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[TRNA|TRNA]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: European rabbit]] | |||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
Revision as of 11:18, 18 July 2018
Structure and assembly pathway of the ribosome quality control complexStructure and assembly pathway of the ribosome quality control complex
Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all. Function[NEMF_HUMAN] Plays a role in nuclear export.[1] [LTN1_HUMAN] E3 ubiquitin-protein ligase. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity). Publication Abstract from PubMedDuring ribosome-associated quality control, stalled ribosomes are split into subunits and the 60S-housed nascent polypeptides are poly-ubiquitinated by Listerin. How this low-abundance ubiquitin ligase targets rare stall-generated 60S among numerous empty 60S is unknown. Here, we show that Listerin specificity for nascent chain-60S complexes depends on nuclear export mediator factor (NEMF). The 3.6 A cryo-EM structure of a nascent chain-containing 60S-Listerin-NEMF complex revealed that NEMF makes multiple simultaneous contacts with 60S and peptidyl-tRNA to sense nascent chain occupancy. Structural and mutational analyses showed that ribosome-bound NEMF recruits and stabilizes Listerin's N-terminal domain, while Listerin's C-terminal RWD domain directly contacts the ribosome to position the adjacent ligase domain near the nascent polypeptide exit tunnel. Thus, highly specific nascent chain targeting by Listerin is imparted by the avidity gained from a multivalent network of context-specific individually weak interactions, highlighting a new principle of client recognition during protein quality control. Structure and Assembly Pathway of the Ribosome Quality Control Complex.,Shao S, Brown A, Santhanam B, Hegde RS Mol Cell. 2015 Jan 7. pii: S1097-2765(14)00964-2. doi:, 10.1016/j.molcel.2014.12.015. PMID:25578875[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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