2y9m: Difference between revisions

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New page: '''Unreleased structure''' The entry 2y9m is ON HOLD until Feb 15 2013 Authors: Williams, C., van den Berg, M., Panjikar, S., Distel, B., Wilmanns, M. Description: Pex4p-Pex22p structu...
 
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'''Unreleased structure'''


The entry 2y9m is ON HOLD  until Feb 15 2013
==Pex4p-Pex22p structure==
<StructureSection load='2y9m' size='340' side='right'caption='[[2y9m]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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='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>
<div style="background-color:#fffaf0;">
== 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.


Authors: Williams, C., van den Berg, M., Panjikar, S., Distel, B., Wilmanns, M.
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<ref>PMID:22085930</ref>


Description: Pex4p-Pex22p structure
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2y9m" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Distel B]]
[[Category: Panjikar S]]
[[Category: Williams C]]
[[Category: Wilmanns M]]
[[Category: Van den Berg M]]

Latest revision as of 01:31, 21 November 2024

Pex4p-Pex22p structure

2y9m, resolution 2.60Å

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