9E0Y
Cryo-EM structure of human cytoplasmic dynein-1 in the presence of ATP
This is a non-PDB format compatible entry.
Summary for 9E0Y
| Entry DOI | 10.2210/pdb9e0y/pdb |
| EMDB information | 47377 |
| Descriptor | Cytoplasmic dynein 1 heavy chain 1, ADENOSINE-5'-DIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | human, motor protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 555995.01 |
| Authors | Nguyen, K.H.V.,Kendrick, A.A.,Leschziner, A.E. (deposition date: 2024-10-20, release date: 2025-07-09, Last modification date: 2026-01-21) |
| Primary citation | Nguyen, K.H.V.,Karasmanis, E.P.,Kendrick, A.A.,Reck-Peterson, S.L.,Leschziner, A.E. Cryo-EM captures early intermediate steps in dynein activation by LIS1. Nat Commun, 16:7054-7054, 2025 Cited by PubMed Abstract: Cytoplasmic dynein-1 (dynein) is an essential molecular motor in eukaryotic cells. Dynein primarily exists in an autoinhibited Phi state and requires conformational changes to assemble with its cofactors and form active transport complexes. LIS1, a key dynein regulator, enhances dynein activation and assembly. Using cryo-EM and a human dynein-LIS1 sample incubated with ATP, we map the conformational landscape of dynein activation by LIS1 and identify an early intermediate state that we propose precedes the previously identified dynein-LIS1 Chi state. Mutations that disrupt this species, which we termed "Pre-Chi", lead to motility defects in vitro, emphasizing its functional importance. Together, our findings provide insights into how LIS1 relieves dynein autoinhibition during the activation pathway. PubMed: 40750582DOI: 10.1038/s41467-025-62185-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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