Is myosin a 'back door' enzyme?

R. G. Yount*, D. Lawson, I. Rayment, L. Yu, C. Berger, H. White, M. Reedy, M. Ferenczi, S. Ishiwata, M. Kushmerick, E. Reisler, S. Highsmith, C. Cremo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

131 Citations (Scopus)

Abstract

ATP has been modeled into the active site of chicken skeletal myosin subfragment-1 using the adenylate kinase · Ap5A structure as a starting reference. The resulting docked ATP · S1 structure is justified in that it rationalizes the photolabeling data from several ATP analogs. The γ- phosphate of ATP sits at the bottom of the active site pocket and is partially visible via a view along the prominent 50-kDa cleft of S1 but not when viewed from above the active site. It is postulated that actin binding promotes the movement of the P-loop and Arg-245 to allow P(i) from ATP to leave via a 'back-door' in the 50-kDa fragment while ADP is still bound at the active site. Such a mechanism can explain a number of experimental observations, including the kinetics of ATP hydrolysis, the nucleotide dependence of P(i) exchange into ATP, and the formation of stable myosin · ADP · vanadate complexes in muscle fibers.

Original languageEnglish
JournalBiophysical Journal
Volume68
Issue number4 SUPPL.
Publication statusPublished - 1995
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics

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