<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Traver MS</submitter><funding>National Institutes of Health</funding><funding>Welch Foundation</funding><funding>NIGMS NIH HHS</funding><funding>NIH HHS</funding><funding>National Science Foundation</funding><pagination>838923</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8922245</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>10</volume><pubmed_abstract>Peroxisomes are eukaryotic organelles that sequester critical oxidative reactions and process the resulting reactive oxygen species into less toxic byproducts. Peroxisome function and formation are coordinated by peroxins (PEX proteins) that guide peroxisome biogenesis and division and shuttle proteins into the lumen and membrane of the organelle. Despite the importance of peroxins in plant metabolism and development, no plant peroxin structures have been reported. Here we report the X-ray crystal structure of the PEX4-PEX22 peroxin complex from the reference plant &lt;i>Arabidopsis thaliana&lt;/i>. PEX4 is a ubiquitin-conjugating enzyme (UBC) that ubiquitinates proteins associated with the peroxisomal membrane, and PEX22 is a peroxisomal membrane protein that anchors PEX4 to the peroxisome and </pubmed_abstract><journal>Frontiers in cell and developmental biology</journal><pubmed_title>The Structure of the &lt;i>Arabidopsis&lt;/i> PEX4-PEX22 Peroxin Complex-Insights Into Ubiquitination at the Peroxisomal Membrane.</pubmed_title><pmcid>PMC8922245</pmcid><funding_grant_id>R01 GM129325</funding_grant_id><funding_grant_id>R35 GM130338</funding_grant_id><funding_grant_id>P30 GM138396</funding_grant_id><funding_grant_id>S10 OD012289</funding_grant_id><pubmed_authors>Traver MS</pubmed_authors><pubmed_authors>Olmos JL</pubmed_authors><pubmed_authors>Phillips GN</pubmed_authors><pubmed_authors>Bradford SE</pubmed_authors><pubmed_authors>Wright ZJ</pubmed_authors><pubmed_authors>Xu W</pubmed_authors><pubmed_authors>Miller MD</pubmed_authors><pubmed_authors>Bartel B</pubmed_authors></additional><is_claimable>false</is_claimable><name>The Structure of the &lt;i>Arabidopsis&lt;/i> PEX4-PEX22 Peroxin Complex-Insights Into Ubiquitination at the Peroxisomal Membrane.</name><description>Peroxisomes are eukaryotic organelles that sequester critical oxidative reactions and process the resulting reactive oxygen species into less toxic byproducts. Peroxisome function and formation are coordinated by peroxins (PEX proteins) that guide peroxisome biogenesis and division and shuttle proteins into the lumen and membrane of the organelle. Despite the importance of peroxins in plant metabolism and development, no plant peroxin structures have been reported. Here we report the X-ray crystal structure of the PEX4-PEX22 peroxin complex from the reference plant &lt;i>Arabidopsis thaliana&lt;/i>. PEX4 is a ubiquitin-conjugating enzyme (UBC) that ubiquitinates proteins associated with the peroxisomal membrane, and PEX22 is a peroxisomal membrane protein that anchors PEX4 to the peroxisome and </description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2026-04-08T17:32:44.449Z</modification><creation>2025-04-04T22:08:56.286Z</creation></dates><accession>S-EPMC8922245</accession><cross_references><pubmed>35300425</pubmed><doi>10.3389/fcell.2022.838923</doi></cross_references></HashMap>