6rlb: Difference between revisions
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The | ==Structure of the dynein-2 complex; tail domain== | ||
<SX load='6rlb' size='340' side='right' viewer='molstar' caption='[[6rlb]], [[Resolution|resolution]] 4.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rlb]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RLB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.5Å</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=6rlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlb OCA], [https://pdbe.org/6rlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rlb RCSB], [https://www.ebi.ac.uk/pdbsum/6rlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B0I1S0_HUMAN B0I1S0_HUMAN] [https://www.uniprot.org/uniprot/E5BBQ0_HUMAN E5BBQ0_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Dynein-2 assembles with polymeric intraflagellar transport (IFT) trains to form a transport machinery that is crucial for cilia biogenesis and signaling. Here we recombinantly expressed the ~1.4-MDa human dynein-2 complex and solved its cryo-EM structure to near-atomic resolution. The two identical copies of the dynein-2 heavy chain are contorted into different conformations by a WDR60-WDR34 heterodimer and a block of two RB and six LC8 light chains. One heavy chain is steered into a zig-zag conformation, which matches the periodicity of the anterograde IFT-B train. Contacts between adjacent dyneins along the train indicate a cooperative mode of assembly. Removal of the WDR60-WDR34-light chain subcomplex renders dynein-2 monomeric and relieves autoinhibition of its motility. Our results converge on a model in which an unusual stoichiometry of non-motor subunits controls dynein-2 assembly, asymmetry, and activity, giving mechanistic insight into the interaction of dynein-2 with IFT trains and the origin of diverse functions in the dynein family. | |||
Structure of the dynein-2 complex and its assembly with intraflagellar transport trains.,Toropova K, Zalyte R, Mukhopadhyay AG, Mladenov M, Carter AP, Roberts AJ Nat Struct Mol Biol. 2019 Sep;26(9):823-829. doi: 10.1038/s41594-019-0286-y. Epub, 2019 Aug 26. PMID:31451806<ref>PMID:31451806</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6rlb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Dynein 3D structures|Dynein 3D structures]] | |||
*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Carter AP]] | |||
[[Category: Mladenov M]] | |||
[[Category: Mukhopadhyay AG]] | |||
[[Category: Roberts AJ]] | |||
[[Category: Toropova K]] | |||
[[Category: Zalyte R]] | |||
Latest revision as of 10:12, 22 May 2024
Structure of the dynein-2 complex; tail domain
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