5H53

The structure of rabbit skeletal muscle actomyosin rigor complex at 5.2 angstrom.

Summary for 5H53

• Entry DOI: 10.2210/pdb5h53/pdb
• EMDB information: 6664
• Descriptor: Skeletal muscle myosin heavy chain MyHC-EO/IIL, Myosin regulatory light chain 2, skeletal muscle isoform type 1, Myosin light chain 1/3, skeletal muscle isoform, ... (5 entities in total)
• Functional Keywords: actin, myosin, muscle, rigor complex, motor protein
• Biological source: Oryctolagus cuniculus (Rabbit); More
• Cellular location: Cytoplasm, cytoskeleton: P68135
• Total number of polymer chains: 5
• Total formula weight: 215070.68

Authors

Fujii, T.,Namba, K. (deposition date: 2016-11-04, release date: 2017-01-18, Last modification date: 2017-01-25)

Primary citation

Fujii, T.,Namba, K.
Structure of actomyosin rigour complex at 5.2 angstrom resolution and insights into the ATPase cycle mechanism
Nat Commun, 8:13969-13969, 2017

PubMed Abstract: Muscle contraction is driven by cyclic association and dissociation of myosin head of the thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin. However, because of the absence of actomyosin rigour structure at high resolution, it still remains unclear how the strong binding of myosin to actin filament triggers the release of hydrolysis products and how ATP binding causes their dissociation. Here we report the structure of mammalian skeletal muscle actomyosin rigour complex at 5.2 Å resolution by electron cryomicroscopy. Comparison with the structures of myosin in various states shows a distinctly large conformational change, providing insights into the ATPase-coupled reaction cycle of actomyosin. Based on our observations, we hypothesize that asymmetric binding along the actin filament could function as a Brownian ratchet by favouring directionally biased thermal motions of myosin and actin.

PubMed: 28067235
DOI: 10.1038/ncomms13969

Experimental method

ELECTRON MICROSCOPY (5.2 Å)