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| - | ==CryoEM structure of dynactin complex at 4.1 angstrom resolution==
| + | #REDIRECT [[5adx]] This PDB entry is obsolete and replaced by 5adx |
| - | <StructureSection load='5aft' size='340' side='right' caption='[[5aft]], [[Resolution|resolution]] 4.00Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[5aft]] is a 27 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa_domesticus Sus scrofa domesticus] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AFT 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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| - | <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='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=5aft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aft OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5aft RCSB], [http://www.ebi.ac.uk/pdbsum/5aft PDBsum]</span></td></tr>
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| - | </table>
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| - | == 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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| - | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | | + | |
| - | ==See Also==
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| - | *[[Dynactin|Dynactin]]
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| - | == References ==
| + | |
| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Sus scrofa]]
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| - | [[Category: Sus scrofa domesticus]]
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| - | [[Category: Carter, A P]]
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| - | [[Category: Diamant, A G]]
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| - | [[Category: Motz, C]]
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| - | [[Category: Patel, N A]]
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| - | [[Category: Robinson, C V]]
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| - | [[Category: Schlage, M A]]
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| - | [[Category: Urnavicius, L]]
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| - | [[Category: Yu, M]]
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| - | [[Category: Zhang, K]]
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| - | [[Category: Actin-like filament]]
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| - | [[Category: Cellular cargo transport]]
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| - | [[Category: Dynactin]]
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| - | [[Category: Dynein co-factor]]
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| - | [[Category: Motor protein]]
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