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
Naturejournal_title
Natureauthors
Schröder RR,Manstein DJ,Jahn W,Holden H,Rayment I,Holmes KC,Spudich JAdoi
10.1038/364171a0subject
Has Abstractpub_date
1993-07-08 00:00:00pages
171-4issue
6433eissn
0028-0836issn
1476-4687journal_volume
364pub_type
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