6rla
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the dynein-2 complex; motor domains== | |
| + | <SX load='6rla' size='340' side='right' viewer='molstar' caption='[[6rla]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6rla]] is a 2 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=6RLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RLA 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]] 3.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6rla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rla OCA], [https://pdbe.org/6rla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rla RCSB], [https://www.ebi.ac.uk/pdbsum/6rla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rla ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/E5BBQ0_HUMAN E5BBQ0_HUMAN] [https://www.uniprot.org/uniprot/B0I1S0_HUMAN B0I1S0_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 6rla" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Dynein 3D structures|Dynein 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]] | ||
Current revision
Structure of the dynein-2 complex; motor domains
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