Figure 2. High-resolution, unidirectional surface metal shadowing of WT GCN4-Kar3Vik1 bound to the surface of microtubules in the presence of ADP. A and B are identical images with the dimeric motor domains indicated with yellow arrows in A, and directly marked with yellow dots in B. Examples of binding of Kar3Vik1 to the microtubule by a single head are indicated with white arrows. The dominant configuration of Kar3Vik1 crosses over two protofilaments. This is strikingly different from dimeric Eg5 (inset: AMPPNP), which predominantly binds with both heads along the same protofilament (see Krzysiak et al., 2006). Unlike other nucleotide states, cooperative binding is not observed. The scale for the insets is the same as in the main panels.
Figure 2.

High-resolution, unidirectional surface metal shadowing of WT GCN4-Kar3Vik1 bound to the surface of microtubules in the presence of ADP. A and B are identical images with the dimeric motor domains indicated with yellow arrows in A, and directly marked with yellow dots in B. Examples of binding of Kar3Vik1 to the microtubule by a single head are indicated with white arrows. The dominant configuration of Kar3Vik1 crosses over two protofilaments. This is strikingly different from dimeric Eg5 (inset: AMPPNP), which predominantly binds with both heads along the same protofilament (see Krzysiak et al., 2006). Unlike other nucleotide states, cooperative binding is not observed. The scale for the insets is the same as in the main panels.

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