Cleft containing reactive thiol of myosin closes during ATP hydrolysis

Sungjo Park, Katalin Ajtai, Thomas P. Burghardt

Research output: Contribution to journalArticle

25 Scopus citations

Abstract

The probe binding cleft of myosin subfragment 1 (S1) contains the reactive thiol, SH1, and tryptophan 510 (Trp-510). Solvent accessibility to Trp-510, measured using the acrylamide quenching of its fluorescence, is highest in rigor and decreases during the ATPase cycle prior to force generation. These data suggest the probe binding cleft closes during ATP hydrolysis and opens during force generation. The closing of the probe binding cleft may be the origin of the shape change of S1 during ATP hydrolysis.

Original languageEnglish (US)
Pages (from-to)1-4
Number of pages4
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1296
Issue number1
DOIs
StatePublished - Aug 15 1996

Keywords

  • ATPase
  • Bent conformation
  • Energy transduction
  • Nucleotide analog
  • Subfragment 1
  • Tryptophan

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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