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6f1u
From Proteopedia
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==N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1== | ==N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1== | ||
| - | < | + | <SX load='6f1u' size='340' side='right' viewer='molstar' caption='[[6f1u]], [[Resolution|resolution]] 3.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6f1u]] is a 13 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6f1u]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F1U FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</td></tr> |
| - | <tr id=' | + | <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></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6f1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f1u OCA], [https://pdbe.org/6f1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f1u RCSB], [https://www.ebi.ac.uk/pdbsum/6f1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f1u ProSAT]</span></td></tr> |
</table> | </table> | ||
| - | == Disease == | ||
| - | [[http://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN]] Autosomal dominant childhood-onset proximal spinal muscular atrophy without contractures;Autosomal dominant non-syndromic intellectual disability;Autosomal dominant Charcot-Marie-Tooth disease type 2O. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ACTZ_PIG ACTZ_PIG] Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules.<ref>PMID:25814576</ref> <ref>PMID:28602352</ref> <ref>PMID:29420470</ref> <ref>PMID:33734450</ref> <ref>PMID:36071160</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 A resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine. | ||
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| + | Cryo-EM shows how dynactin recruits two dyneins for faster movement.,Urnavicius L, Lau CK, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP Nature. 2018 Feb 7;554(7691):202-206. doi: 10.1038/nature25462. PMID:29420470<ref>PMID:29420470</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6f1u" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Actin-related protein 3D structures|Actin-related protein 3D structures]] | ||
| + | *[[Dynactin|Dynactin]] | ||
| + | *[[Dynein 3D structures|Dynein 3D structures]] | ||
| + | *[[F-actin capping protein|F-actin capping protein]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| - | [[Category: Carter | + | [[Category: Carter AP]] |
| - | [[Category: Elshenawy | + | [[Category: Elshenawy MM]] |
| - | [[Category: Lau | + | [[Category: Lau CK]] |
| - | [[Category: Morales-Rios | + | [[Category: Morales-Rios E]] |
| - | [[Category: Motz | + | [[Category: Motz C]] |
| - | [[Category: Urnavicius | + | [[Category: Urnavicius L]] |
| - | [[Category: Yildiz | + | [[Category: Yildiz A]] |
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Current revision
N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1
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Categories: Homo sapiens | Large Structures | Mus musculus | Sus scrofa | Carter AP | Elshenawy MM | Lau CK | Morales-Rios E | Motz C | Urnavicius L | Yildiz A
