7PMD
Cryo-EM structure of the actomyosin-V complex in the post-rigor transition state (AppNHp, central 1er)
Summary for 7PMD
| Entry DOI | 10.2210/pdb7pmd/pdb |
| Related | 7PLT 7PM5 7PME 7PMF 7PMG 7PMH 7PMI 7PMJ 7PML |
| EMDB information | 13529 |
| Related PRD ID | PRD_002366 |
| Descriptor | Unconventional myosin-Va, Actin, alpha skeletal muscle, Phalloidin, ... (7 entities in total) |
| Functional Keywords | motor protein, myosin, cytoskeleton, f-actin, phalloidin |
| Biological source | Gallus gallus (Chicken) More |
| Total number of polymer chains | 4 |
| Total formula weight | 152379.41 |
| Authors | Pospich, S.,Sweeney, H.L.,Houdusse, A.,Raunser, S. (deposition date: 2021-09-02, release date: 2021-12-22) |
| Primary citation | Pospich, S.,Sweeney, H.L.,Houdusse, A.,Raunser, S. High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Elife, 10:-, 2021 Cited by PubMed Abstract: The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are only partially understood, mostly due to sparse structural data on actin-bound states of myosin. Here, we report 26 high-resolution cryo-EM structures of the actomyosin-V complex in the strong-ADP, rigor, and a previously unseen post-rigor transition state that binds the ATP analog AppNHp. The structures reveal a high flexibility of myosin in each state and provide valuable insights into the structural transitions of myosin-V upon ADP release and binding of AppNHp, as well as the actomyosin interface. In addition, they show how myosin is able to specifically alter the structure of F-actin. PubMed: 34812732DOI: 10.7554/eLife.73724 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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