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| | ==Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp90 peptide== | | ==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=''> | + | <StructureSection load='4i2z' size='340' side='right'caption='[[4i2z]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i2z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. 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> | + | <table><tr><td colspan='2'>[[4i2z]] is a 2 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=4I2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i2w|4i2w]]</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=4i2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i2z OCA], [https://pdbe.org/4i2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i2z RCSB], [https://www.ebi.ac.uk/pdbsum/4i2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i2z ProSAT]</span></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 CAEEL])</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=4i2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i2z OCA], [http://pdbe.org/4i2z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i2z RCSB], [http://www.ebi.ac.uk/pdbsum/4i2z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i2z ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HSP90_CAEEL HSP90_CAEEL]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required to stabilize the daf-11/transmembrane guanylyl cyclases or another signal transduction component that regulates cGMP levels. Participates in the control of cell cycle progression at the prophase/metaphase transition in oocyte development by ensuring the activity of wee-1.3 kinase, which negatively regulates cdk-1 through its phosphorylation.<ref>PMID:10790386</ref> <ref>PMID:16466390</ref> | + | [https://www.uniprot.org/uniprot/G5EG62_CAEEL G5EG62_CAEEL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| - | [[Category: Clausen, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Gazda, L]] | + | [[Category: Clausen T]] |
| - | [[Category: Hellerschmied, D]] | + | [[Category: Gazda L]] |
| - | [[Category: Chaperone]] | + | [[Category: Hellerschmied D]] |
| - | [[Category: Chaperone-protein binding complex]]
| + | |
| - | [[Category: Hsp70 and hsp90 co-chaperone]]
| + | |
| - | [[Category: Myofilament formation]]
| + | |
| - | [[Category: Myosin folding]]
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| - | [[Category: Protein filament]]
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| - | [[Category: Tpr-peptide interaction]]
| + | |
| - | [[Category: Ucs domain containing protein]]
| + | |
| Structural highlights
Function
G5EG62_CAEEL
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gazda L, Pokrzywa W, Hellerschmied D, Lowe T, Forne I, Mueller-Planitz F, Hoppe T, Clausen T. The myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans. Cell. 2013 Jan 17;152(1-2):183-95. doi: 10.1016/j.cell.2012.12.025. PMID:23332754 doi:http://dx.doi.org/10.1016/j.cell.2012.12.025
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