8E00
Symmetry expansion of yeast cytoplasmic dynein-1 bound to Lis1 in the chi conformation.
Summary for 8E00
| Entry DOI | 10.2210/pdb8e00/pdb |
| Related | 7MGM 8DZZ |
| EMDB information | 27810 27811 |
| Descriptor | Dynein heavy chain, cytoplasmic, Nuclear distribution protein PAC1, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | dynein, motor protein, transport |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 3 |
| Total formula weight | 447533.98 |
| Authors | Reimer, J.M.,Lahiri, I.,Leschziner, A.E. (deposition date: 2022-08-08, release date: 2023-08-30, Last modification date: 2023-09-27) |
| Primary citation | Karasmanis, E.P.,Reimer, J.M.,Kendrick, A.A.,Nguyen, K.H.V.,Rodriguez, J.A.,Truong, J.B.,Lahiri, I.,Reck-Peterson, S.L.,Leschziner, A.E. Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge. Nat.Struct.Mol.Biol., 30:1357-1364, 2023 Cited by PubMed Abstract: Cytoplasmic dynein-1 transports intracellular cargo towards microtubule minus ends. Dynein is autoinhibited and undergoes conformational changes to form an active complex that consists of one or two dynein dimers, the dynactin complex, and activating adapter(s). The Lissencephaly 1 gene, LIS1, is genetically linked to the dynein pathway from fungi to mammals and is mutated in people with the neurodevelopmental disease lissencephaly. Lis1 is required for active dynein complexes to form, but how it enables this is unclear. Here, we present a structure of two yeast dynein motor domains with two Lis1 dimers wedged in-between. The contact sites between dynein and Lis1 in this structure, termed 'Chi,' are required for Lis1's regulation of dynein in Saccharomyces cerevisiae in vivo and the formation of active human dynein-dynactin-activating adapter complexes in vitro. We propose that this structure represents an intermediate in dynein's activation pathway, revealing how Lis1 relieves dynein's autoinhibited state. PubMed: 37620585DOI: 10.1038/s41594-023-01069-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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