Is myosin a "back door" enzyme?


Journal Article

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 gamma-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 Pi 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 Pi exchange into ATP, and the formation of stable myosin.ADP.vanadate complexes in muscle fibers.

Full Text

Cited Authors

  • Yount, RG; Lawson, D; Rayment, I

Published Date

  • April 1995

Published In

Volume / Issue

  • 68 / 4 Suppl

Start / End Page

  • 44S - 47S

PubMed ID

  • 7787099

Pubmed Central ID

  • 7787099

International Standard Serial Number (ISSN)

  • 0006-3495


  • eng

Conference Location

  • United States