8PR5
Structure of the autoinhibited dynactin p150glued projection
This is a non-PDB format compatible entry.
Summary for 8PR5
| Entry DOI | 10.2210/pdb8pr5/pdb |
| EMDB information | 2855 |
| Descriptor | Dynactin subunit 1 (1 entity in total) |
| Functional Keywords | dynactin, p150, lis1, motor protein |
| Biological source | Sus scrofa (pig) |
| Total number of polymer chains | 2 |
| Total formula weight | 190888.42 |
| Authors | Singh, K.,Lau, C.K.,Manigrasso, G.,Gassmann, R.,Carter, A.P. (deposition date: 2023-07-12, release date: 2024-03-27, Last modification date: 2024-04-10) |
| Primary citation | Singh, K.,Lau, C.K.,Manigrasso, G.,Gama, J.B.,Gassmann, R.,Carter, A.P. Molecular mechanism of dynein-dynactin complex assembly by LIS1. Science, 383:eadk8544-eadk8544, 2024 Cited by PubMed Abstract: Cytoplasmic dynein is a microtubule motor vital for cellular organization and division. It functions as a ~4-megadalton complex containing its cofactor dynactin and a cargo-specific coiled-coil adaptor. However, how dynein and dynactin recognize diverse adaptors, how they interact with each other during complex formation, and the role of critical regulators such as lissencephaly-1 (LIS1) protein (LIS1) remain unclear. In this study, we determined the cryo-electron microscopy structure of dynein-dynactin on microtubules with LIS1 and the lysosomal adaptor JIP3. This structure reveals the molecular basis of interactions occurring during dynein activation. We show how JIP3 activates dynein despite its atypical architecture. Unexpectedly, LIS1 binds dynactin's p150 subunit, tethering it along the length of dynein. Our data suggest that LIS1 and p150 constrain dynein-dynactin to ensure efficient complex formation. PubMed: 38547289DOI: 10.1126/science.adk8544 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8.6 Å) |
Structure validation
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