Strain Mediated Adaptation Is Key for Myosin Mechanochemistry: Discovering General Rules for Motor Activity
Fig 3
Structural adaptation of the trailing head signals faster ADP release.
(A) Myosin MH domain structure showing the big (red) and small (green) subunits. (B) Nucleotide binding region of the MH domain is shown in terms of P-loop (blue), switch I (red) and switch II (green). (C) RMSD distribution (P(RMSD)) of the small subunit of the MH domain after least square fitting of the big subunit from the leading and trailing head simulations. The RMSD is calculated with respect to the pre-powerstroke MH conformation. Note the larger RMSD for the trailing head indicating substantial structural changes. (D) Distribution of distances between P-loop and switch I (P(dSWI-Ploop)) for the leading and trailing head simulations. (E) Distribution of distances between P-loop and switch II (P(dSWII-Ploop)) for the leading and trailing head simulations. (F) Distribution of distances between switch I and switch II (P(dSWI-SWII)) for the leading and trailing head simulations. A larger distance between switch I and switch II for the trailing head simulation compared to leading head signals faster ADP release.