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7t92

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Current revision (13:07, 1 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7t92]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothelomyces_thermophilus_ATCC_42464 Thermothelomyces thermophilus ATCC 42464] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T92 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7t92]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothelomyces_thermophilus_ATCC_42464 Thermothelomyces thermophilus ATCC 42464] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T92 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=LBN:1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine'>LBN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=LBN:1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine'>LBN</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=7t92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t92 OCA], [https://pdbe.org/7t92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t92 RCSB], [https://www.ebi.ac.uk/pdbsum/7t92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t92 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=7t92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t92 OCA], [https://pdbe.org/7t92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t92 RCSB], [https://www.ebi.ac.uk/pdbsum/7t92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t92 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/G2Q5N0_MYCTT G2Q5N0_MYCTT]]
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[https://www.uniprot.org/uniprot/G2Q5N0_MYCTT G2Q5N0_MYCTT]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Peroxisomes are ubiquitous organelles that house various metabolic reactions and are essential for human health(1-4). Luminal peroxisomal proteins are imported from the cytosol by mobile receptors, which then recycle back to the cytosol by a poorly understood process(1-4). Recycling requires receptor modification by a membrane-embedded ubiquitin ligase complex comprising three RING finger domain-containing proteins (Pex2, Pex10 and Pex12)(5,6). Here we report a cryo-electron microscopy structure of the ligase complex, which together with biochemical and in vivo experiments reveals its function as a retrotranslocation channel for peroxisomal import receptors. Each subunit of the complex contributes five transmembrane segments that co-assemble into an open channel. The three ring finger domains form a cytosolic tower, with ring finger 2 (RF2) positioned above the channel pore. We propose that the N terminus of a recycling receptor is inserted from the peroxisomal lumen into the pore and monoubiquitylated by RF2 to enable extraction into the cytosol. If recycling is compromised, receptors are polyubiquitylated by the concerted action of RF10 and RF12 and degraded. This polyubiquitylation pathway also maintains the homeostasis of other peroxisomal import factors. Our results clarify a crucial step during peroxisomal protein import and reveal why mutations in the ligase complex cause human disease.
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A peroxisomal ubiquitin ligase complex forms a retrotranslocation channel.,Feng P, Wu X, Erramilli SK, Paulo JA, Knejski P, Gygi SP, Kossiakoff AA, Rapoport TA Nature. 2022 Jun 29. pii: 10.1038/s41586-022-04903-x. doi:, 10.1038/s41586-022-04903-x. PMID:35768507<ref>PMID:35768507</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7t92" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Structure of the peroxisomal retro-translocon formed by a heterotrimeric ubiquitin ligase complex

PDB ID 7t92

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