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  The structure of the rigor complex and its implications for the power stroke

Holmes, K. C., Schröder, R. R., Sweeney, H. L., & Houdusse, A. (2004). The structure of the rigor complex and its implications for the power stroke. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, 359(1452), 1819-1828. doi:10.1098/rstb.2004.1566.

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Genre: Journal Article
Alternative Title : The structure of the rigor complex and its implications for the power stroke

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PhilTransRoySocB_359_2004_1819.pdf (Any fulltext), 3MB
 
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 Creators:
Holmes, Kenneth C.1, Author              
Schröder, Rasmus R.1, 2, Author              
Sweeney, H. L., Author
Houdusse, Anne, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: strong binding; actin; myosin cross-bridge; myosin V; decorated actin; cryo-energy-filter electron microscopy
 Abstract: Decorated actin provides a model system for studying the strong interaction between actin and myosin. Cryo-energy-filter electron microscopy has recently yielded a 14 A resolution map of rabbit skeletal actin decorated with chicken skeletal S1. The crystal structure of the cross-bridge from skeletal chicken myosin could not be fitted into the three-dimensional electron microscope map without some deformation. However, a newly published structure of the nucleotide-free myosin V cross-bridge, which is apparently already in the strong binding form, can be fitted into the three-dimensional reconstruction without distortion. This supports the notion that nucleotide-free myosin V is an excellent model for strongly bound myosin and allows us to describe the actin-myosin interface. In myosin V the switch 2 element is closed although the lever arm is down (post-power stroke). Therefore, it appears likely that switch 2 does not open very much during the power stroke. The myosin V structure also differs from the chicken skeletal myosin structure in the nucleotide-binding site and the degree of bending of the backbone ß-sheet. These suggest a mechanism for the control of the power stroke by strong actin binding.

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Language(s): eng - English
 Dates: 2004-12-29
 Publication Status: Published in print
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 Rev. Type: Peer
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Title: Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
Source Genre: Journal
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Publ. Info: London : Royal Society
Pages: - Volume / Issue: 359 (1452) Sequence Number: - Start / End Page: 1819 - 1828 Identifier: ISSN: 0962-8436
CoNE: https://pure.mpg.de/cone/journals/resource/963017382021_1