5h53

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

Loading... Status: waiting for Mol* initialization Structural highlights 5h53 is a 5 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 5.2Å Ligands: ADP, HIC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9GJP9_RABIT Publication Abstract from PubMed 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 A 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. Structure of actomyosin rigour complex at 5.2 A resolution and insights into the ATPase cycle mechanism.,Fujii T, Namba K Nat Commun. 2017 Jan 9;8:13969. doi: 10.1038/ncomms13969. PMID:28067235 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Actin 3D structures Myosin 3D Structures

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