JCB logo
R&D Systems
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 23 December 2002. doi:10.1083/jcb.200208172
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 307K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Burgess, S.
Right arrow Articles by Trinick, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Burgess, S.
Right arrow Articles by Trinick, J.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*HomoloGene*UniGene
*Compound via MeSH
*Substance via MeSH
Related Collections
Right arrowRelated Article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
© The Rockefeller University Press, 0021-9525/2002/12/983 $5.00
The Journal of Cell Biology, Volume 159, Number 6, 983-991

Article

 The prepower stroke conformation of myosin V

Stan Burgess1, Matt Walker1, Fei Wang2, James R. Sellers2, Howard D. White3, Peter J. Knight1 and John Trinick1

1 Astbury Centre for Structural Molecular Biology and School of Biomedical Sciences, University of Leeds, Leeds, LS2 9JT, UK
2 Laboratory of Molecular Cardiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892
3 Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, VA 23507

Address correspondence to J. Trinick, School of Biomedical Sciences, Leeds University, Leeds LS2 9JT, UK. Tel./Fax: 44-113-343-4350. E-mail: j.trinick{at}leeds.ac.uk

eW have used electron microscopy and single-particle image processing to study head conformation in myosin V molecules. We find that in the presence of ATP, many heads have a sharply angled conformation that is rare in its absence. The sharply angled conformation is similar to a myosin II atomic structure proposed to mimic the prepower stroke state. The leading head in molecules attached to actin by both heads has a similar conformation, but is also sharply angled in a second plane by tethering through the trail head. The lead head lever joins the motor domain ~5 nm axially from where it joins the trail motor. These positions locate the converter subdomain and show the lead motor is in the prepower stroke conformation. Tethering by the trail head places the lead head motor domain at the correct axial position along the actin for binding, but at the wrong orientation. Attachment is achieved either by bending the lead head lever throughout its length or at the pliant point. The microscopy shows that most of the walking stride is produced by changes in lever angle brought about by converter movement, but is augmented by distortion produced by thermal energy.

Key Words: titling lever; force; thermal ratchet; mechanism; walking


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?

Related Article

How to start a motor
Alan W. Dove
J. Cell Biol. 2002 159: 911. [Full Text] [PDF]



This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents