EMD-11315

Single-particle
4.05 Å
EMD-11315 Deposition: 06/07/2020
Map released: 29/07/2020
Last modified: 28/04/2021
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-11315

The pointed end complex of dynactin, with accompanying Arp1/actin filament subunits

EMD-11315

Single-particle
4.05 Å
EMD-11315 Deposition: 06/07/2020
Map released: 29/07/2020
Last modified: 28/04/2021
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Sus scrofa
Sample: Dynactin complex

Deposition Authors: Lau CK, Lacey SE, Carter AP
Cryo-EM reveals the complex architecture of dynactin's shoulder region and pointed end.
Lau CK , O'Reilly FJ , Santhanam B , Lacey SE , Rappsilber J , Carter AP
(2021) Embo J. , 40 , e106164 - e106164
PUBMED: 33734450
DOI: doi:10.15252/embj.2020106164
ISSN: 1460-2075
ASTM: EMJODG
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.