Nucleotide trapping at the ATPase site of myosin subfragment 1 by a new interthiol crosslinking

Proc Natl Acad Sci U S A. 1986 Apr;83(7):2037-41. doi: 10.1073/pnas.83.7.2037.

Abstract

When myosin subfragment 1 derivatives in which the reactive sulfhydryl SH1 has been blocked react with N,N'-p-phenylenedimaleimide or 5,5'-dithiobis(2-nitrobenzoic acid), the reactive sulfhydryl group SH2 of the 20-kDa domain is crosslinked with a thiol of the 50-kDa domain of the heavy chain. The crosslink induces the stable trapping of a significant amount of Mg2+-nucleotide in the ATPase site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenine Nucleotides / metabolism*
  • Adenosine Triphosphatases / antagonists & inhibitors
  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Binding Sites
  • Calcium-Transporting ATPases / metabolism
  • In Vitro Techniques
  • Kinetics
  • Macromolecular Substances
  • Magnesium / metabolism
  • Myosin Subfragments
  • Myosins / metabolism*
  • Peptide Fragments / metabolism*
  • Rabbits
  • Sulfhydryl Compounds
  • Sulfhydryl Reagents / pharmacology

Substances

  • Adenine Nucleotides
  • Macromolecular Substances
  • Myosin Subfragments
  • Peptide Fragments
  • Sulfhydryl Compounds
  • Sulfhydryl Reagents
  • Adenosine Triphosphatases
  • Myosins
  • Calcium-Transporting ATPases
  • Magnesium