» Articles » PMID: 34812732

High-resolution Structures of the Actomyosin-V Complex in Three Nucleotide States Provide Insights into the Force Generation Mechanism

Overview
Journal Elife
Specialty Biology
Date 2021 Nov 23
PMID 34812732
Citations 20
Authors
Affiliations
Soon will be listed here.
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.

Citing Articles

High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory.

Chavali S, Carman P, Shuman H, Ostap E, Sindelar C Proc Natl Acad Sci U S A. 2025; 122(9):e2415457122.

PMID: 40014570 PMC: 11892617. DOI: 10.1073/pnas.2415457122.


High resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory.

Chavali S, Carman P, Shuman H, Ostap E, Sindelar C bioRxiv. 2025; .

PMID: 39829824 PMC: 11741418. DOI: 10.1101/2025.01.10.632429.


Myosin forces elicit an F-actin structural landscape that mediates mechanosensitive protein recognition.

Carl A, Reynolds M, Gurel P, Phua D, Sun X, Mei L bioRxiv. 2024; .

PMID: 39185238 PMC: 11343212. DOI: 10.1101/2024.08.15.608188.


Insights into Actin Isoform-Specific Interactions with Myosin via Computational Analysis.

Yu C, Park Y, An M, Ryu B, Jung H Molecules. 2024; 29(13).

PMID: 38998944 PMC: 11242942. DOI: 10.3390/molecules29132992.


Switch-2 determines MgADP-release kinetics and fine-tunes the duty ratio of class-1 myosins.

Diensthuber R, Hartmann F, Kathmann D, Franz P, Tsiavaliaris G Front Physiol. 2024; 15:1393952.

PMID: 38887318 PMC: 11181000. DOI: 10.3389/fphys.2024.1393952.


References
1.
Adams P, Afonine P, Bunkoczi G, Chen V, Echols N, Headd J . The Phenix software for automated determination of macromolecular structures. Methods. 2011; 55(1):94-106. PMC: 3193589. DOI: 10.1016/j.ymeth.2011.07.005. View

2.
Chen V, Arendall 3rd W, Headd J, Keedy D, Immormino R, Kapral G . MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr. 2010; 66(Pt 1):12-21. PMC: 2803126. DOI: 10.1107/S0907444909042073. View

3.
Doran M, Pavadai E, Rynkiewicz M, Walklate J, Bullitt E, Moore J . Cryo-EM and Molecular Docking Shows Myosin Loop 4 Contacts Actin and Tropomyosin on Thin Filaments. Biophys J. 2020; 119(4):821-830. PMC: 7451941. DOI: 10.1016/j.bpj.2020.07.006. View

4.
Cai L, Makhov A, Bear J . F-actin binding is essential for coronin 1B function in vivo. J Cell Sci. 2007; 120(Pt 10):1779-90. DOI: 10.1242/jcs.007641. View

5.
Laskowski R . PDBsum new things. Nucleic Acids Res. 2008; 37(Database issue):D355-9. PMC: 2686501. DOI: 10.1093/nar/gkn860. View