Structural studies of myosin:nucleotide complexes: a revised model for the molecular basis of muscle contraction.

Journal Article

The structures of the MgADP-beryllium fluoride and MgADP-aluminum fluoride complexes of the truncated myosin head from Dictyostelium myosin II are reported. These reveal the location of the nucleotide complex and define the amino acid residues that form the active site. The tertiary structure of the beryllium fluoride complex is essentially identical to that seen previously in the three-dimensional structure of chicken skeletal muscle myosin. By contrast, significant domain movements are observed in the aluminum fluoride complex. These structural findings form the basis of a revised model for the structural basis of the contractile cycle. It is now suggested that the narrow cleft that splits the central 50-kDa segment of the heavy chain provides not only the communication route between the nucleotide-binding pocket and actin but also transmits the conformational change necessary for movement.

Duke Authors

Cited Authors

  • Fisher, AJ; Smith, CA; Thoden, J; Smith, R; Sutoh, K; Holden, HM; Rayment, I

Published Date

  • April 1995

Published In

Volume / Issue

  • 68 / 4 Suppl

Start / End Page

  • 19S - 26S

PubMed ID

  • 7787065

Electronic International Standard Serial Number (EISSN)

  • 1542-0086

International Standard Serial Number (ISSN)

  • 0006-3495

Language

  • eng