Journal
CELL
Volume 102, Issue 5, Pages 683-694Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(00)00090-8
Keywords
-
Categories
Funding
- NATIONAL CENTER FOR RESEARCH RESOURCES [S06RR008110] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES [P01AR042895] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM035154] Funding Source: NIH RePORTER
- NCRR NIH HHS [RR-08110] Funding Source: Medline
- NIAMS NIH HHS [AR42895] Funding Source: Medline
- NIGMS NIH HHS [GM-35154] Funding Source: Medline
Ask authors/readers for more resources
The molecular motor myosin is proposed to bind to actin and swing its light-chain binding region through a large angle to produce an similar to 10 nm step in motion coupled to changes in the nucleotide state at the active site. To date, however, direct dynamic measurements have largely failed to show changes of that magnitude. Here, we use a cysteine engineering approach to create a high resolution, FRET-based sensor that reports a large, similar to 70 degree nucleotide-dependent angle change of the light-chain binding region. The combination of steady-state and time-resolved fluorescence resonance energy transfer measurements unexpectedly reveals two distinct prestroke states. The measurements also show that bound Mg.ADP.P-i, and not bound Mg.ATP, induces the myosin to adopt the prestroke states.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available