Cleft containing reactive thiol of myosin closes during ATP hydrolysis.
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.
Park
S
S
Department of Biochemistry and Molecular Biology, Mayo Foundation, Rochester, MN 55905, USA.
Ajtai
K
K
Burghardt
T P
TP
D000255:Adenosine Triphosphate / Q000378:metabolism*; D001665:Binding Sites; D003545:Cysteine / Q000737:chemistry* / Q000378:metabolism; D006868:Hydrolysis; D008958:Models, Molecular; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D013050:Spectrometry, Fluorescence / Q000379:methods; D014364:Tryptophan / Q000737:chemistry / Q000378:metabolism
D014364:Tryptophan; D000255:Adenosine Triphosphate; D009218:Myosins; D003545:Cysteine