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© Research
Publication : Proceedings of the National Academy of Sciences of the United States of America

Myosin isoforms show unique conformations in the actin-bound state.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proceedings of the National Academy of Sciences of the United States of America - 18 Mar 2003

Volkmann N, Ouyang G, Trybus KM, DeRosier DJ, Lowey S, Hanein D,

Link to Pubmed [PMID] – 12612343

Proc Natl Acad Sci U S A 2003 Mar; 100(6): 3227-32

Crystallographic data for several myosin isoforms have provided evidence for at least two conformations in the absence of actin: a prehydrolysis state that is similar to the original nucleotide-free chicken skeletal subfragment-1 (S1) structure, and a transition-state structure that favors hydrolysis. These weak-binding states differ in the extent of closure of the cleft that divides the actin-binding region of the myosin and the position of the light chain binding domain or lever arm that is believed to be associated with force generation. Previously, we provided insights into the interaction of smooth-muscle S1 with actin by computer-based fitting of crystal structures into three-dimensional reconstructions obtained by electron cryomicroscopy. Here, we analyze the conformations of actin-bound chicken skeletal muscle S1. We conclude that both myosin isoforms in the nucleotide-free, actin-bound state can achieve a more tightly closed cleft, a more downward position of the lever arm, and more stable surface loops than those seen in the available crystal structures, indicating the existence of unique actin-bound conformations.

https://pubmed.ncbi.nlm.nih.gov/12612343