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PMID: 1869586 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Three-dimensional structure of myosin subfragment-1 from electron microscopy of sectioned crystals.

The Journal of cell biology ·Vol. 114 ·No. 4 ·1991-08-00 ·Pages 701-13

Winkelmann DA, Baker TS, Rayment I

Abstract

Image analysis of electron micrographs of thin-sectioned myosin subfragment-1 (S1) crystals has been used to determine the structure of the myosin head at approximately 25-A resolution. Previous work established that the unit cell of type I crystals of myosin S1 contains eight molecules arranged with orthorhombic space group symmetry P212121 and provided preliminary information on the size and shape of the myosin head (Winkelmann, D. A., H. Mekeel, and I. Rayment. 1985. J. Mol. Biol. 181:487-501). We have applied a systematic method of data collection by electron microscopy to reconstruct the three-dimensional (3D) structure of the S1 crystal lattice. Electron micrographs of thin sections were recorded at angles of up to 50 degrees by tilting the sections about the two orthogonal unit cell axes in sections cut perpendicular to the three major crystallographic axes. The data from six separate tilt series were merged to form a complete data set for 3D reconstruction. This approach has yielded an electron density map of the unit cell of the S1 crystals of sufficient detail. to delineate the molecular envelope of the myosin head. Myosin S1 has a tadpole-shaped molecular envelope that is very similar in appearance to the pear-shaped myosin heads observed by electron microscopy of rotary-shadowed and negatively stained myosin. The molecule is divided into essentially three morphological domains: a large domain on one end of the molecule corresponding to approximately 60% of the total molecular volume, a smaller central domain of approximately 30% of the volume that is separated from the larger domain by a cleft on one side of the molecule, and the smallest domain corresponding to a thin tail-like region containing approximately 10% of the volume. This molecular organization supports models of force generation by myosin which invoke conformational mobility at interdomain junctions within the head.

MeSH Terms
Actomyosin/ultrastructure Animals Chickens Microscopy, Electron Models, Molecular Muscles Myosin Subfragments/isolation & purification,ultrastructure Myosins/ultrastructure Protein Conformation
Chemicals
Myosin Subfragments Actomyosin Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Winkelmann D A
Department of Pathology, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Baker T S
Rayment I
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.114.4.701
Published
1991-08-00
Pages
701-13
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2289899
Subset
IM
Grants
NIAMS NIH HHS · R01 AR038454 · United States
NIAMS NIH HHS · AR35186 · United States
NIAMS NIH HHS · R01 AR035186 · United States
NIGMS NIH HHS · GM33050 · United States
NIAMS NIH HHS · AR38454 · United States
External Links
PubMed source DOI: 10.1083/jcb.114.4.701 PMC Full Text View journal details
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