Myosin-V as a mechanical sensor: an elastic network study.
According to recent experiments, the molecular-motor myosin behaves like a strain sensor, exhibiting different functional responses when loads in opposite directions are applied to its tail. Within an elastic-network model, we explore the sensitivity of the protein to the forces acting on the tail and find, in agreement with experiments, that such forces invoke conformational changes that should affect filament binding and ADP release. Furthermore, conformational responses of myosin to the application of forces to individual residues in its principal functional regions are systematically investigated and a detailed sensitivity map of myosin-V is thus obtained. The results suggest that the strain-sensor behavior is involved in the intrinsic operation of this molecular motor.
Department of Physical Chemistry, Fritz Haber Institute of the Max Planck Society, Berlin, Germany. duettmann@fhi-berlin.mpg.de
Markus
M
Düttmann
Yuichi
Y
Togashi
Toshio
T
Yanagida
Alexander S
AS
Mikhailov
D000199:Actins / Q000378:metabolism; D000244:Adenosine Diphosphate / Q000378:metabolism; D001665:Binding Sites; D001696:Biomechanical Phenomena; D004548:Elasticity; D008958:Models, Molecular; D024701:Myosin Type V / Q000737:chemistry* / Q000378:metabolism*; D009711:Nucleotides / Q000378:metabolism; D011487:Protein Conformation
D000199:Actins; D009711:Nucleotides; D000244:Adenosine Diphosphate; D024701:Myosin Type V