Journal
JOURNAL OF CELL BIOLOGY
Volume 177, Issue 3, Pages 377-385Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200612090
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Funding
- NIGMS NIH HHS [P01 GM051487, R01 GM046033, GM46033, GM51487] Funding Source: Medline
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We have used cryo-electron microscopy of kinesin-decorated microtubules to resolve the structure of the motor protein kinesin's crucial nucleotide response elements, switch I and the switch II helix, in kinesin's poorly understood nucleotide-free state. Both of the switch elements undergo conformational change relative to the microtubule-free state. The changes in switch I suggest a role for it in ejecting adenosine diphosphate when kinesin initially binds to the microtubule. The switch II helix has an N-terminal extension, apparently stabilized by conserved microtubule contacts, implying a microtubule activation mechanism that could convey the state of the bound nucleotide to kinesin's putative force-delivering element (the neck linker). In deriving this structure, we have adapted an image-processing technique, single-particle reconstruction, for analyzing decorated microtubules. The resulting reconstruction visualizes the asymmetric seam present in native, 13-protofilament microtubules, and this method will provide an avenue to higher-resolution characterization of a variety of microtubule-binding proteins, as well as the microtubule itself.
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