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==Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp70 peptide== | |||
<StructureSection load='4i2w' size='340' side='right' caption='[[4i2w]], [[Resolution|resolution]] 3.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4i2w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I2W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I2W FirstGlance]. <br> | |||
</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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i2z|4i2z]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">unc-45, CELE_F30H5.1, F30H5.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])</td></tr> | |||
<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=4i2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i2w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i2w RCSB], [http://www.ebi.ac.uk/pdbsum/4i2w PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The UCS (UNC-45/CRO1/She4) chaperones play an evolutionarily conserved role in promoting myosin-dependent processes, including cytokinesis, endocytosis, RNA transport, and muscle development. To investigate the protein machinery orchestrating myosin folding and assembly, we performed a comprehensive analysis of Caenorhabditis elegans UNC-45. Our structural and biochemical data demonstrate that UNC-45 forms linear protein chains that offer multiple binding sites for cooperating chaperones and client proteins. Accordingly, Hsp70 and Hsp90, which bind to the TPR domain of UNC-45, could act in concert and with defined periodicity on captured myosin molecules. In vivo analyses reveal the elongated canyon of the UCS domain as a myosin-binding site and show that multimeric UNC-45 chains support organization of sarcomeric repeats. In fact, expression of transgenes blocking UNC-45 chain formation induces dominant-negative defects in the sarcomere structure and function of wild-type worms. Together, these findings uncover a filament assembly factor that directly couples myosin folding with myofilament formation. | |||
The myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans.,Gazda L, Pokrzywa W, Hellerschmied D, Lowe T, Forne I, Mueller-Planitz F, Hoppe T, Clausen T Cell. 2013 Jan 17;152(1-2):183-95. doi: 10.1016/j.cell.2012.12.025. PMID:23332754<ref>PMID:23332754</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Heat Shock Proteins|Heat Shock Proteins]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Clausen, T | [[Category: Clausen, T]] | ||
[[Category: Gazda, L | [[Category: Gazda, L]] | ||
[[Category: Hellerschmied, D | [[Category: Hellerschmied, D]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Chaperone-protein binding complex]] | [[Category: Chaperone-protein binding complex]] | ||
