5mzu

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m (Protected "5mzu" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5mzu is ON HOLD
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==Crystal structure of the myosin chaperone UNC-45 from C. elegans (alternative conformation)==
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<StructureSection load='5mzu' size='340' side='right' caption='[[5mzu]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5mzu]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MZU FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i2z|4i2z]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mzu OCA], [http://pdbe.org/5mzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mzu RCSB], [http://www.ebi.ac.uk/pdbsum/5mzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mzu ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Hellerschmied, D., Gazda, L., Clausen, T.
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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>
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Description: Crystal structure of the myosin chaperone UNC-45 from C. elegans (alternative conformation)
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5mzu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Clausen, T]]
[[Category: Clausen, T]]
[[Category: Gazda, L]]
[[Category: Gazda, L]]
[[Category: Hellerschmied, D]]
[[Category: Hellerschmied, D]]
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[[Category: Arm repeat]]
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[[Category: Chaperone]]
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[[Category: Myosin folding]]
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[[Category: Protein filament]]
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[[Category: Ucs domain]]

Revision as of 06:22, 15 February 2018

Crystal structure of the myosin chaperone UNC-45 from C. elegans (alternative conformation)

5mzu, resolution 3.80Å

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