4a7n 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.
[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Publication Abstract from PubMed
Regulation of myosin and filamentous actin interaction by tropomyosin is a central feature of contractile events in muscle and nonmuscle cells. However, little is known about molecular interactions within the complex and the trajectory of tropomyosin movement between its "open" and "closed" positions on the actin filament. Here, we report the 8 A resolution structure of the rigor (nucleotide-free) actin-tropomyosin-myosin complex determined by cryo-electron microscopy. The pseudoatomic model of the complex, obtained from fitting crystal structures into the map, defines the large interface involving two adjacent actin monomers and one tropomyosin pseudorepeat per myosin contact. Severe forms of hereditary myopathies are linked to mutations that critically perturb this interface. Myosin binding results in a 23 A shift of tropomyosin along actin. Complex domain motions occur in myosin, but not in actin. Based on our results, we propose a structural model for the tropomyosin-dependent modulation of myosin binding to actin.
Structure of the rigor actin-tropomyosin-Myosin complex.,Behrmann E, Muller M, Penczek PA, Mannherz HG, Manstein DJ, Raunser S Cell. 2012 Jul 20;150(2):327-38. PMID:22817895[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Behrmann E, Muller M, Penczek PA, Mannherz HG, Manstein DJ, Raunser S. Structure of the rigor actin-tropomyosin-Myosin complex. Cell. 2012 Jul 20;150(2):327-38. PMID:22817895 doi:10.1016/j.cell.2012.05.037
