Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1.
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.
Schröder
R R
RR
Biophysics Department, Max-Planck-Institute for Medical Research, Heidelberg, Germany.
Manstein
D J
DJ
Jahn
W
W
Holden
H
H
Rayment
I
I
Holmes
K C
KC
Spudich
J A
JA
D000199:Actins / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D004023:Dictyostelium; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015879:Myosin Subfragments / Q000737:chemistry*; D011485:Protein Binding; D011817:Rabbits; D011994:Recombinant Proteins / Q000737:chemistry
D000199:Actins; D015879:Myosin Subfragments; D011994:Recombinant Proteins