Abstract:
:The molecular motor protein myosin VI moves toward the minus-end of actin filaments with a step size of 30-36 nm. Such large step size either drastically limits the degree of complex formation between dimer subunits to leave enough length for the lever arms, or requires an extension of the lever arms' crystallographically observed structure. Recent experimental work proposed that myosin VI dimerization triggers the unfolding of the protein's proximal tail domain which could drive the needed lever-arm extension. Here, we demonstrate through steered molecular dynamics simulation the feasibility of sufficient extension arising from turning a three-helix bundle into a long α-helix. A key role is played by the known calmodulin binding that facilitates the extension by altering the strain path in myosin VI. Sequence analysis of the proximal tail domain suggests that further calmodulin binding sites open up when the domain's three-helix bundle is unfolded and that subsequent calmodulin binding stabilizes the extended lever arms.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Liu Y,Hsin J,Kim H,Selvin PR,Schulten Kdoi
10.1016/j.bpj.2011.05.010subject
Has Abstractpub_date
2011-06-22 00:00:00pages
2964-73issue
12eissn
0006-3495issn
1542-0086pii
S0006-3495(11)00580-7journal_volume
100pub_type
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