7t9x

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7t9x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T9X FirstGlance]. <br>
<table><tr><td colspan='2'>[[7t9x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T9X 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=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">X-ray diffraction, [[Resolution|Resolution]] 1.52&#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=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=7t9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t9x OCA], [https://pdbe.org/7t9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t9x RCSB], [https://www.ebi.ac.uk/pdbsum/7t9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t9x 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=7t9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t9x OCA], [https://pdbe.org/7t9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t9x RCSB], [https://www.ebi.ac.uk/pdbsum/7t9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t9x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PEX12_YEAST PEX12_YEAST]] Required for protein import into peroxisomes.
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[https://www.uniprot.org/uniprot/PEX12_YEAST PEX12_YEAST] Required for protein import into peroxisomes.
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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 7t9x" 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

Saccharomyces cerevisiae Pex12 RING domain

PDB ID 7t9x

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