This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3j92
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==Structure and assembly pathway of the ribosome quality control complex== | ==Structure and assembly pathway of the ribosome quality control complex== | ||
| - | < | + | <SX load='3j92' size='340' side='right' viewer='molstar' caption='[[3j92]], [[Resolution|resolution]] 3.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3j92]] is a | + | <table><tr><td colspan='2'>[[3j92]] 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=3J92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J92 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j92 OCA], [https://pdbe.org/3j92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j92 RCSB], [https://www.ebi.ac.uk/pdbsum/3j92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j92 ProSAT]</span></td></tr> |
</table> | </table> | ||
| - | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/NEMF_HUMAN NEMF_HUMAN]] Plays a role in nuclear export.<ref>PMID:16103875</ref> [[http://www.uniprot.org/uniprot/LTN1_HUMAN 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). | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | During 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<ref>PMID:25578875</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]] | |
| - | == | + | |
| - | + | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
| + | [[Category: Large Structures]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
| - | + | [[Category: Brown A]] | |
| - | [[Category: Brown | + | [[Category: Hegde RS]] |
| - | [[Category: Hegde | + | [[Category: Santhanam B]] |
| - | [[Category: Santhanam | + | [[Category: Shao S]] |
| - | [[Category: Shao | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Structure and assembly pathway of the ribosome quality control complex
| |||||||||
