Reference: Kikkawa M, et al. (2000) 15 A resolution model of the monomeric kinesin motor, KIF1A. Cell 100(2):241-52

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Abstract


A two-headed structure has been widely believed to be essential for the kinesin molecular motor to move processively on the track, microtubules. However, we have recently demonstrated that a monomeric motor domain construct of KIF1A (C351), a kinesin superfamily protein, moves processively, taking about 700 steps before being detached from microtubules. To elucidate the mechanism of its single-headed processivity, we examined the C351 -MT interaction by mutant analysis and high-resolution cryo-EM. Mutant analysis indicated the importance of a highly positively charged loop, the "K loop," for such processivity. A 15 A resolution structure unambiguously docked with the available atomic models revealed "K loop" as an extra microtubule-binding domain specific to KIF1A, and bound to the C terminus of tubulin. The site-specific cross-linking further confirmed this model.

Reference Type
Comparative Study | Journal Article | Research Support, Non-U.S. Gov't
Authors
Kikkawa M, Okada Y, Hirokawa N
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