5mzu
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the myosin chaperone UNC-45 from C. elegans (alternative conformation)== | |
| + | <StructureSection load='5mzu' size='340' side='right'caption='[[5mzu]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mzu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MZU 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]] 3.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5mzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mzu OCA], [https://pdbe.org/5mzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mzu RCSB], [https://www.ebi.ac.uk/pdbsum/5mzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mzu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/G5EG62_CAEEL G5EG62_CAEEL] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Muscle development requires the coordinated activities of specific protein folding and degradation factors. UFD-2, a U-box ubiquitin ligase, has been reported to play a central role in this orchestra regulating the myosin chaperone UNC-45. Here, we apply an integrative in vitro and in vivo approach to delineate the substrate-targeting mechanism of UFD-2 and elucidate its distinct mechanistic features as an E3/E4 enzyme. Using Caenorhabditis elegans as model system, we demonstrate that UFD-2 is not regulating the protein levels of UNC-45 in muscle cells, but rather shows the characteristic properties of a bona fide E3 ligase involved in protein quality control. Our data demonstrate that UFD-2 preferentially targets unfolded protein segments. Moreover, the UNC-45 chaperone can serve as an adaptor protein of UFD-2 to poly-ubiquitinate unfolded myosin, pointing to a possible role of the UFD-2/UNC-45 pair in maintaining proteostasis in muscle cells. | ||
| - | + | UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins.,Hellerschmied D, Roessler M, Lehner A, Gazda L, Stejskal K, Imre R, Mechtler K, Dammermann A, Clausen T Nat Commun. 2018 Feb 2;9(1):484. doi: 10.1038/s41467-018-02924-7. PMID:29396393<ref>PMID:29396393</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Clausen | + | <div class="pdbe-citations 5mzu" style="background-color:#fffaf0;"></div> |
| - | [[Category: Gazda | + | == References == |
| - | [[Category: Hellerschmied | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Caenorhabditis elegans]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Clausen T]] | ||
| + | [[Category: Gazda L]] | ||
| + | [[Category: Hellerschmied D]] | ||
Current revision
Crystal structure of the myosin chaperone UNC-45 from C. elegans (alternative conformation)
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