Suppressed By

V29D
Y118F
E150K[F3]
K462T
Q480H
T647M
P650T
I656F

WHERE: W501 occurs in the bend that follows the CamShaft.

WHAT: This residue apparently participates in a key transition of the myosin structure. It is thought to be the tryptophan whose fluorescence undergoes a change during the motor cycle, indicative of an alteration of its environment. Biochemically it features enhanced basal (idling) ATPase and shows essentially NO activation of ATPase in the presence of actin (working ATPase). It fials to move actin filaments on its own, and interferes with the ability of wild-type myosin motors to do so.

FRIENDS & RELATIONS: W501L is one of the original cold-senstive mutants. In three dimensions, the sidechain of W501 comes into close proximity to the sidechains of Y494K[I5] and G691C[G7]. It also shares a number of suppressors with these two mutations (including E150K[F3], T647M[G7], P650T[F7] and I656F[F6]). Preliminary results indicate that L453F [E7] and N483S[G7], two suppressors of G680V[G7] may also tap into this suppressor family.

Image: W501L is a primary mutant in the CamShaft Mirror