6qdk: Difference between revisions
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==Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin== | |||
<StructureSection load='6qdk' size='340' side='right'caption='[[6qdk]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6qdk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QDK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QDK 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>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qdl|6qdl]], [[6qdm|6qdm]]</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=6qdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qdk OCA], [http://pdbe.org/6qdk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qdk RCSB], [http://www.ebi.ac.uk/pdbsum/6qdk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qdk ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Myosin is a motor protein that is essential for a variety of processes ranging from intracellular transport to muscle contraction. Folding and assembly of myosin relies on a specific chaperone, UNC-45. To address its substrate-targeting mechanism, we reconstitute the interplay between Caenorhabditis elegans UNC-45 and muscle myosin MHC-B in insect cells. In addition to providing a cellular chaperone assay, the established system enabled us to produce large amounts of functional muscle myosin, as evidenced by a biochemical and structural characterization, and to directly monitor substrate binding to UNC-45. Data from in vitro and cellular chaperone assays, together with crystal structures of binding-deficient UNC-45 mutants, highlight the importance of utilizing a flexible myosin-binding domain. This so-called UCS domain can adopt discrete conformations to efficiently bind and fold substrate. Moreover, our data uncover the molecular basis of temperature-sensitive UNC-45 mutations underlying one of the most prominent motility defects in C. elegans. | |||
Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin.,Hellerschmied D, Lehner A, Franicevic N, Arnese R, Johnson C, Vogel A, Meinhart A, Kurzbauer R, Deszcz L, Gazda L, Geeves M, Clausen T Nat Commun. 2019 Oct 21;10(1):4781. doi: 10.1038/s41467-019-12667-8. PMID:31636255<ref>PMID:31636255</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6qdk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Clausen, T]] | [[Category: Clausen, T]] | ||
[[Category: Hellerschmied, D]] | [[Category: Hellerschmied, D]] | ||
[[Category: Meinhart, A]] | [[Category: Meinhart, A]] | ||
[[Category: Chaperone]] | |||
[[Category: Myofilament formation]] | |||
[[Category: Myosin folding]] | |||
[[Category: Protein filament]] | |||
