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

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. Here we report an atomic model for the actomyosin complex produced by combining the atomic X-ray structure of F-actin and chicken myosin S1 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.

journal_name

Nature

journal_title

Nature

authors

Schröder RR,Manstein DJ,Jahn W,Holden H,Rayment I,Holmes KC,Spudich JA

doi

10.1038/364171a0

subject

Has Abstract

pub_date

1993-07-08 00:00:00

pages

171-4

issue

6433

eissn

0028-0836

issn

1476-4687

journal_volume

364

pub_type

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