E150K[F3] |
Suppresses L453F
[E7]^ * = suppression is reciprocal |
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WHERE: E150K is 'flapping in the breeze'. If the whale had an occipital bone, this would be it. The side chain is solvent-exposed (i.e. on the very outside of the molecule) and doesn't seem to be close to ANYthing--in the known crystal structures! Perhaps is achieves greater proximity at a heretofore unseen point (see below). WHAT: A charge reversal (negative glutamic acid (E) to positive Lysine (K)). Capable of suppression three clustered cold-sensitive mutations, Y494K[I5], W501L and G691C (all near the end of the Camshaft which is at residue 496), as well as Cluster member L453F [E7]. Change to Lysine does not seem to perturb myosin function in vivo as measured by plaque expansion rates (hence its list is of mutants that it suppresses, since it is itself healthy and doe not require suppression). Preliminary biochemistry hints it is a 'supermyosin' in terms of ATPase--it 'rests' with lower turnover (= less waste) than wild type, but runs hotter in the presence of actin. However, results in the contractility assay suggest it is nonetheless inferior as a cytoskeletal motor. FRIENDS & RELATIONS: In its ability to suppress mutants shown and its lack of in vivo phenotype it is similar to L94F, Y118F, P650T, I656F and others. It is spatially not unrelated to F85S,L and Y118F. Image: E150K can be found in the CamShaftSupps mirror.
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| Bruce Patterson http://research.biology.arizona.edu/myosin |
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