6ZNO
The pointed end complex of dynactin with the p150 projection docked
Summary for 6ZNO
| Entry DOI | 10.2210/pdb6zno/pdb |
| Related | 6ZO4 |
| EMDB information | 11313 11314 11315 11316 11317 11318 11319 |
| Descriptor | ARP1 actin related protein 1 homolog A, ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ... (12 entities in total) |
| Functional Keywords | dynactin, complex, scaffold, cytoskeleton, structural protein |
| Biological source | Sus scrofa (Pig) More |
| Total number of polymer chains | 10 |
| Total formula weight | 343359.53 |
| Authors | Lau, C.K.,Lacey, S.E.,Carter, A.P. (deposition date: 2020-07-06, release date: 2020-07-29, Last modification date: 2024-05-01) |
| Primary citation | Lau, C.K.,O'Reilly, F.J.,Santhanam, B.,Lacey, S.E.,Rappsilber, J.,Carter, A.P. Cryo-EM reveals the complex architecture of dynactin's shoulder region and pointed end. Embo J., 40:e106164-e106164, 2021 Cited by PubMed Abstract: Dynactin is a 1.1 MDa complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In order to do this, it forms a tripartite complex with dynein and a coiled-coil adaptor. Dynactin consists of an actin-related filament whose length is defined by its flexible shoulder domain. Despite previous cryo-EM structures, the molecular architecture of the shoulder and pointed end of the filament is still poorly understood due to the lack of high-resolution information in these regions. Here we combine multiple cryo-EM datasets and define precise masking strategies for particle signal subtraction and 3D classification. This overcomes domain flexibility and results in high-resolution maps into which we can build the shoulder and pointed end. The unique architecture of the shoulder securely houses the p150 subunit and positions the four identical p50 subunits in different conformations to bind dynactin's filament. The pointed end map allows us to build the first structure of p62 and reveals the molecular basis for cargo adaptor binding to different sites at the pointed end. PubMed: 33734450DOI: 10.15252/embj.2020106164 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.8 Å) |
Structure validation
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