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  Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1

Schröder, R. R., Manstein, D. J., Jahn, W., Holden, H. M., Rayment, I., Holmes, K. C., et al. (1993). Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1. Nature, 364, 171-174. doi:10.1038/364171a0.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-AA2D-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-26B6-E
Genre: Journal Article

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Nature_364_1993_171.pdf (Any fulltext), 860KB
 
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 Creators:
Schröder, Rasmus R.1, 2, Author              
Manstein, Dietmar J.2, 3, Author              
Jahn, Werner2, 4, Author              
Holden, Hazel M., Author
Rayment, Ivan, Author
Holmes, Kenneth C.2, 4, 5, Author              
Spudich, James A., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
3Dietmar Manstein Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497708              
4Muscle Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497731              
5Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society, ou_1497735              

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 Abstract: ELUCIDATION of the molecular contacts between actin and myosin is central to understanding the force-generating process in muscle and other cells. Actin, a highly conserved globular protein found in all eukaryotes, polymerizes into filaments (F-actin) for most of its biological functions. Myosins, which are more diverse in sequence, share a conserved globular head of about 900 amino acids in length (subfragment-1 or S1) at the N-terminal end of the molecule. S1 contains all the elements necessary for mechano-chemical force transduction in vitro 1,2. Here we report an atomic model for the actomyosin complex produced by combining the atomic X-ray structure of F-actin3,4 and chicken myosin S15 with a three-dimensional reconstruction from electron micrographs of frozen-hydrated F-actin decorated with recombinant Dictyostelium myosin S1. The accuracy of the reconstruction shows the position of actin and myosin molecules unambiguously.

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Language(s): eng - English
 Dates: 1993-01-081993-04-261993-07-08
 Publication Status: Published in print
 Pages: 4
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 Rev. Type: Peer
 Identifiers: eDoc: 665082
DOI: 10.1038/364171a0
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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 364 Sequence Number: - Start / End Page: 171 - 174 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238