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The myosin II coiled-coil domain atomic structure in its native environment

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America
 [1];  [2];  [3];  [1];  [3];  [2];  [4];  [5];  [3]
  1. Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380,, Department of Physics, Florida State University, Tallahassee, FL 32306-4380,
  2. Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA 92093,
  3. Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380,
  4. Department of Biological Sciences, Illinois Institute of Technology, Chicago, IL 60616,
  5. Department of Cell Biology, Duke University Medical Center, Durham, NC 27607

Significance

Myosin II is the molecule that produces force in muscle contraction. Unlike the myosin head, its molecular motor, no atomic resolution structure of the ∼1000-residue–long α-helical coiled-coil tail has been reported. Here, we describe the cryo-EM atomic structure of the myosin tail within a native muscle thick filament. Three differences with crystal structures of myosin tail segments were found. The myosin head arrangement apparently alters the beginning of the tail. Striated muscle myosins have four skip residues, amino acids inserted to improve the alignment of charged residue clusters. Skips 1 and 3 agree with the crystal structures. Skip 2, which is a novel structure, and Skip 4 do not. Functional consequences are suggested by the myosin tail packing.

Sponsoring Organization:
USDOE
Grant/Contract Number:
AC02-06CH11357
OSTI ID:
1773201
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 14 Vol. 118; ISSN 0027-8424
Publisher:
Proceedings of the National Academy of SciencesCopyright Statement
Country of Publication:
United States
Language:
English

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