4a7n: Difference between revisions
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==Structure of bare F-actin filaments obtained from the same sample as the Actin-Tropomyosin-Myosin Complex== | ==Structure of bare F-actin filaments obtained from the same sample as the Actin-Tropomyosin-Myosin Complex== | ||
<StructureSection load='4a7n' size='340' side='right' caption='[[4a7n]], [[Resolution|resolution]] 8.90Å' scene=''> | <StructureSection load='4a7n' size='340' side='right'caption='[[4a7n]], [[Resolution|resolution]] 8.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a7n]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A7N FirstGlance]. <br> | <table><tr><td colspan='2'>[[4a7n]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A7N FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Actin|Actin]] | *[[Actin 3D structures|Actin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:54, 6 March 2019
Structure of bare F-actin filaments obtained from the same sample as the Actin-Tropomyosin-Myosin ComplexStructure of bare F-actin filaments obtained from the same sample as the Actin-Tropomyosin-Myosin Complex
Structural highlights
Function[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 PubMedRegulation 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. See AlsoReferences
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