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- Title
Structure of a kinesin-tubulin complex and implications for kinesin motility.
- Authors
Gigant, Benoît; Wang, Weiyi; Dreier, Birgit; Jiang, Qiyang; Pecqueur, Ludovic; Plückthun, Andreas; Wang, Chunguang; Knossow, Marcel
- Abstract
The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of the conformational changes that lead to the power stroke that moves a kinesin's load along a microtubule, we determined the X-ray structure of human kinesin-1 bound to αβ-tubulin. The structure defines the mechanism of microtubule-stimulated ATP hydrolysis, which releases the kinesin motor domain from microtubules. It also reveals the structural linkages that connect the ATP nucleotide to the kinesin neck linker, a 15-amino acid segment C terminal to the catalytic core of the motor domain, to result in the power stroke. ATP binding to the microtubule-bound kinesin favors neck-linker docking. This biases the attachment of kinesin's second head in the direction of the movement, thus initiating each of the steps taken.
- Subjects
KINESIN; ADENOSINE triphosphate; MICROTUBULES; HYDROLYSIS; TUBULINS; NUCLEOTIDES; AMINO acids
- Publication
Nature Structural & Molecular Biology, 2013, Vol 20, Issue 8, p1001
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.2624