4i2z
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp90 peptide== | |
| - | + | <StructureSection load='4i2z' size='340' side='right' caption='[[4i2z]], [[Resolution|resolution]] 2.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4i2z]] 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=4I2Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I2Z 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">[[4i2w|4i2w]]</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=4i2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i2z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i2z RCSB], [http://www.ebi.ac.uk/pdbsum/4i2z 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> | ||
| + | == 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]] | ||
Revision as of 08:30, 18 December 2014
Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp90 peptide
| |||||||||||
