5afu

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==Cryo-EM structure of dynein tail-dynactin-BICD2N complex==
==Cryo-EM structure of dynein tail-dynactin-BICD2N complex==
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<StructureSection load='5afu' size='340' side='right' caption='[[5afu]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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<SX load='5afu' size='340' side='right' viewer='molstar' caption='[[5afu]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5afu]] is a 33 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AFU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5afu]] is a 19 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AFU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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<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></td></tr>
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<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=5afu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5afu RCSB], [http://www.ebi.ac.uk/pdbsum/5afu PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5afu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afu OCA], [https://pdbe.org/5afu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5afu RCSB], [https://www.ebi.ac.uk/pdbsum/5afu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5afu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACTB_PIG ACTB_PIG]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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[https://www.uniprot.org/uniprot/A0A0J9X2A1_PIG A0A0J9X2A1_PIG]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Dynactin is an essential cofactor for the microtubule motor cytoplasmic dynein-1. We report the structure of the 23-subunit dynactin complex by cryo-electron microscopy to 4.0 angstroms. Our reconstruction reveals how dynactin is built around a filament containing eight copies of the actin-related protein Arp1 and one of beta-actin. The filament is capped at each end by distinct protein complexes, and its length is defined by elongated peptides that emerge from the alpha-helical shoulder domain. A further 8.2 angstrom structure of the complex between dynein, dynactin, and the motility-inducing cargo adaptor Bicaudal-D2 shows how the translational symmetry of the dynein tail matches that of the dynactin filament. The Bicaudal-D2 coiled coil runs between dynein and dynactin to stabilize the mutually dependent interactions between all three components.
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The structure of the dynactin complex and its interaction with dynein.,Urnavicius L, Zhang K, Diamant AG, Motz C, Schlager MA, Yu M, Patel NA, Robinson CV, Carter AP Science. 2015 Mar 27;347(6229):1441-6. doi: 10.1126/science.aaa4080. Epub 2015, Feb 12. PMID:25814576<ref>PMID:25814576</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5afu" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Dynactin|Dynactin]]
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*[[Dynein 3D structures|Dynein 3D structures]]
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*[[F-actin capping protein|F-actin capping protein]]
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== References ==
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<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Carter, A P]]
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[[Category: Carter AP]]
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[[Category: Diamant, A G]]
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[[Category: Diamant AG]]
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[[Category: Motz, C]]
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[[Category: Motz C]]
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[[Category: Patel, N A]]
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[[Category: Patel NA]]
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[[Category: Robinson, C V]]
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[[Category: Robinson CV]]
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[[Category: Schlager, M A]]
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[[Category: Schlager MA]]
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[[Category: Urnavicius, L]]
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[[Category: Urnavicius L]]
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[[Category: Yu, M]]
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[[Category: Yu M]]
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[[Category: Zhang, K]]
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[[Category: Zhang K]]
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[[Category: Bicd2]]
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[[Category: Dynactin]]
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[[Category: Dynein]]
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[[Category: Motor]]
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[[Category: Motor protein]]
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[[Category: Transport]]
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Current revision

Cryo-EM structure of dynein tail-dynactin-BICD2N complex

5afu, resolution 3.50Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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