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3j92

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Revision as of 13:28, 4 May 2022

Structure and assembly pathway of the ribosome quality control complex

3j92, resolution 3.60Å

Structural highlights

3j92 is a 55 chain structure with sequence from European rabbit, Oryctolagus cuniculus and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	NEMF, SDCCAG1 (European rabbit), LTN1, C21orf10, C21orf98, KIAA0714, RNF160, ZNF294, HSPC087 (European rabbit)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bi X, Jones T, Abbasi F, Lee H, Stultz B, Hursh DA, Mortin MA. Drosophila caliban, a nuclear export mediator, can function as a tumor suppressor in human lung cancer cells. Oncogene. 2005 Dec 15;24(56):8229-39. PMID:16103875 doi:http://dx.doi.org/10.1038/sj.onc.1208962
↑ Shao S, Brown A, Santhanam B, Hegde RS. Structure and Assembly Pathway of the Ribosome Quality Control Complex. Mol Cell. 2015 Jan 7. pii: S1097-2765(14)00964-2. doi:, 10.1016/j.molcel.2014.12.015. PMID:25578875 doi:http://dx.doi.org/10.1016/j.molcel.2014.12.015

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3j92"

@@ Line 3: / Line 3: @@
 <SX load='3j92' size='340' side='right' viewer='molstar' caption='[[3j92]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
 == Structural highlights ==
-<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://proteopedia.org/fgij/fg.htm?mol=3J92 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3j92]] is a 55 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit], [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3J92 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NEMF, SDCCAG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit]), LTN1, C21orf10, C21orf98, KIAA0714, RNF160, ZNF294, HSPC087 ([https://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://proteopedia.org/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>
+<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>
 == 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).
+[[https://www.uniprot.org/uniprot/NEMF_HUMAN NEMF_HUMAN]] Plays a role in nuclear export.<ref>PMID:16103875</ref>  [[https://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 ==

3j92

From Proteopedia

Revision as of 13:28, 4 May 2022

Structure and assembly pathway of the ribosome quality control complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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