7z8m
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7z8m]] is a 9 chain structure with sequence from [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=7Z8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z8M FirstGlance]. <br> | <table><tr><td colspan='2'>[[7z8m]] is a 9 chain structure with sequence from [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=7Z8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z8M FirstGlance]. <br> | ||
| - | </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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.37Å</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7z8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z8m OCA], [https://pdbe.org/7z8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z8m RCSB], [https://www.ebi.ac.uk/pdbsum/7z8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z8m ProSAT]</span></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=7z8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z8m OCA], [https://pdbe.org/7z8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z8m RCSB], [https://www.ebi.ac.uk/pdbsum/7z8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z8m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== 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 == | ||
| + | Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor(1-3). Up to two dynein dimers can be recruited per dynactin, and interactions between them affect their combined motile behaviour(4-6). Different coiled-coil adaptors are linked to different cargos(7,8), and some share motifs known to contact sites on dynein and dynactin(4,9-13). There is limited structural information on how the resulting complex interacts with microtubules and how adaptors are recruited. Here we develop a cryo-electron microscopy processing pipeline to solve the high-resolution structure of dynein-dynactin and the adaptor BICDR1 bound to microtubules. This reveals the asymmetric interactions between neighbouring dynein motor domains and how they relate to motile behaviour. We found that two adaptors occupy the complex. Both adaptors make similar interactions with the dyneins but diverge in their contacts with each other and dynactin. Our structure has implications for the stability and stoichiometry of motor recruitment by cargos. | ||
| + | |||
| + | Structure of dynein-dynactin on microtubules shows tandem adaptor binding.,Chaaban S, Carter AP Nature. 2022 Oct;610(7930):212-216. doi: 10.1038/s41586-022-05186-y. Epub 2022 , Sep 7. PMID:36071160<ref>PMID:36071160</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7z8m" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Actin-related protein 3D structures|Actin-related protein 3D structures]] | *[[Actin-related protein 3D structures|Actin-related protein 3D structures]] | ||
| + | *[[Dynactin|Dynactin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
The pointed end complex of dynactin bound to BICDR1
| |||||||||||
