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  Structure of the rigor actin-tropomyosin-myosin complex

Behrmann, E., Müller, M., Penczek, P. A., Mannherz, H. G., Manstein, D. J., & Raunser, S. (2012). Structure of the rigor actin-tropomyosin-myosin complex. Cell, 150(2), 327-338. doi:10.1016/j.cell.2012.05.037.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-63DA-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-63DB-C
Genre: Journal Article

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Behrmann, E.1, Author
Müller, M., Author
Penczek, P. A., Author
Mannherz, H. G., Author
Manstein, D. J., Author
Raunser, S., Author
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1External Organizations, ou_persistent22              

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Free keywords: Actins/*chemistry/genetics/metabolism Animals Cryoelectron Microscopy Humans Models, Molecular Multiprotein Complexes/*chemistry/genetics/metabolism Muscle, Skeletal/metabolism Muscular Diseases/genetics/metabolism Myosins/chemistry/genetics/*metabolism Rabbits Tropomyosin/*chemistry/genetics/metabolism
 Abstract: 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.

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 Dates: 2012
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: Other: 22817895
DOI: 10.1016/j.cell.2012.05.037
ISSN: 1097-4172 (Electronic)
ISSN: 0092-8674 (Linking)
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Title: Cell
  Alternative Title : Cell
Source Genre: Journal
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Pages: - Volume / Issue: 150 (2) Sequence Number: - Start / End Page: 327 - 338 Identifier: -