Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1925857 | Archives of Biochemistry and Biophysics | 2011 | 7 Pages |
Abstract
⺠The compound 2,4-dinitrophenol (DNP) binds near a helix-loop-helix that includes a reactive lysine (Lys553) in myosin's lower 50-kDa subdomain, activating ATP hydrolysis. ⺠Reactivity of this lysine is reduced differentially by a broad range of ligands (nucleotide analogs, actin and DNP), indicating significant conformational flexibility among subdomains along the entire pathway from ATP pocket to the actin-binding region. ⺠Lys553 reactivity appears to be correlated with progressive closure of the 50-kDa cleft rather than changes in the status of switch 2. We suggest the DNP stabilizes the cleft in a partially open state.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Theresa R. Bomfim, Luciana E.S.F. Machado, Luis Mauricio T.R. Lima, Martha M. Sorenson, Verônica P. Salerno,