6qdk: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 6qdk is ~~ON HOLD until Paper~~ Publication

==Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin==

== Structural highlights ==

<table><tr><td colspan='2'>[[6qdk]] is a 1 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=6QDK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QDK FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6qdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qdk OCA], [https://pdbe.org/6qdk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qdk RCSB], [https://www.ebi.ac.uk/pdbsum/6qdk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qdk ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/G5EG62_CAEEL G5EG62_CAEEL]

== 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.

~~Authors:~~ Meinhart, A., Clausen, T.~~, Hellerschmied, D~~.

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>

~~Description: Molecular features~~ of the ~~UNC~~-~~45 chaperone critical for binding and folding muscle myosin~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: Clausen, T]]

[[Category: Hellerschmied, D]]

== References ==

[[Category: Meinhart, A]]

__TOC__

</StructureSection>

[[Category: Caenorhabditis elegans]]

[[Category: Large Structures]]

[[Category: Clausen T]]

[[Category: Hellerschmied D]]

[[Category: Meinhart A]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6qdk is ON HOLD  until Paper Publication
+==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]] 3.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6qdk]] is a 1 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=6QDK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QDK FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6qdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qdk OCA], [https://pdbe.org/6qdk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qdk RCSB], [https://www.ebi.ac.uk/pdbsum/6qdk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qdk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/G5EG62_CAEEL G5EG62_CAEEL]
+<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.
-Authors: Meinhart, A., Clausen, T., Hellerschmied, D.
+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>
-Description: Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Clausen, T]]
+<div class="pdbe-citations 6qdk" style="background-color:#fffaf0;"></div>
-[[Category: Hellerschmied, D]]
+== References ==
-[[Category: Meinhart, A]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Caenorhabditis elegans]]
+[[Category: Large Structures]]
+[[Category: Clausen T]]
+[[Category: Hellerschmied D]]
+[[Category: Meinhart A]]