7z8i: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7z8i]] is a 17 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=7Z8I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z8I FirstGlance]. <br> | <table><tr><td colspan='2'>[[7z8i]] is a 17 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=7Z8I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z8I 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=MG:MAGNESIUM+ION'>MG</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]] 3.3Å</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=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=7z8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z8i OCA], [https://pdbe.org/7z8i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z8i RCSB], [https://www.ebi.ac.uk/pdbsum/7z8i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z8i 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=7z8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z8i OCA], [https://pdbe.org/7z8i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z8i RCSB], [https://www.ebi.ac.uk/pdbsum/7z8i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z8i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/DC1I2_HUMAN DC1I2_HUMAN] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCNT1. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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 | 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> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 7z8i" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7z8i" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Dynactin|Dynactin]] | |||
*[[Dynein 3D structures|Dynein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||