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| | <StructureSection load='2y9m' size='340' side='right'caption='[[2y9m]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='2y9m' size='340' side='right'caption='[[2y9m]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2y9m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y9M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y9m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y9M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2y9o|2y9o]], [[2y9p|2y9p]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=2y9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y9m OCA], [https://pdbe.org/2y9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y9m RCSB], [https://www.ebi.ac.uk/pdbsum/2y9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y9m 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=2y9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y9m OCA], [https://pdbe.org/2y9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y9m RCSB], [https://www.ebi.ac.uk/pdbsum/2y9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y9m ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/UBCX_YEAST UBCX_YEAST]] Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis. Required for UBC4-independent ubiquitination of PEX5. [[https://www.uniprot.org/uniprot/PEX22_YEAST PEX22_YEAST]] Involved in peroxisome biogenesis (By similarity).
| + | [https://www.uniprot.org/uniprot/UBCX_YEAST UBCX_YEAST] Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis. Required for UBC4-independent ubiquitination of PEX5. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ubiquitin--protein ligase]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Berg, M van den]]
| + | [[Category: Distel B]] |
| - | [[Category: Distel, B]] | + | [[Category: Panjikar S]] |
| - | [[Category: Panjikar, S]] | + | [[Category: Williams C]] |
| - | [[Category: Williams, C]] | + | [[Category: Wilmanns M]] |
| - | [[Category: Wilmanns, M]] | + | [[Category: Van den Berg M]] |
| - | [[Category: Alpha-beta-alpha sandwich fold]] | + | |
| - | [[Category: E2 co-activator]]
| + | |
| - | [[Category: E2 complex]]
| + | |
| - | [[Category: Ligase-transport protein complex]]
| + | |
| - | [[Category: Peroxisomal protein]]
| + | |
| - | [[Category: Ubiquitin conjugating enzyme]]
| + | |
| Structural highlights
Function
UBCX_YEAST Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis. Required for UBC4-independent ubiquitination of PEX5.
Publication Abstract from PubMed
Ubiquitin-conjugating enzymes (E2s) coordinate distinct types of ubiquitination via specific E3 ligases, to a large number of protein substrates. While many E2 enzymes need only the presence of an E3 ligase for substrate ubiquitination, a number of E2s require additional, non-canonical binding partners to specify their function. Here, we have determined the crystal structure and function of an E2/co-activator assembly, the Pex4p:Pex22p complex. The peroxisome-associated E2 enzyme Pex4p binds the peroxisomal membrane protein Pex22p through a binding site that does not overlap with any other known interaction interface in E2 enzymes. Pex22p association enhances Pex4p's ability to transfer ubiquitin to a substrate in vitro, and Pex22p binding-deficient forms of Pex4p are unable to ubiquitinate the peroxisomal import receptor Pex5p in vivo. Our data demonstrate that the Pex4p:Pex22p assembly, and not Pex4p alone, functions as the E2 enzyme required for Pex5p ubiquitination, establishing a novel mechanism of E2 enzyme regulation.
Insights into ubiquitin-conjugating enzyme/ co-activator interactions from the structure of the Pex4p:Pex22p complex.,Williams C, van den Berg M, Panjikar S, Stanley WA, Distel B, Wilmanns M EMBO J. 2011 Nov 15. doi: 10.1038/emboj.2011.411. PMID:22085930[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Williams C, van den Berg M, Panjikar S, Stanley WA, Distel B, Wilmanns M. Insights into ubiquitin-conjugating enzyme/ co-activator interactions from the structure of the Pex4p:Pex22p complex. EMBO J. 2011 Nov 15. doi: 10.1038/emboj.2011.411. PMID:22085930 doi:10.1038/emboj.2011.411
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