title: Structure of a kinesin-tubulin complex and implications for kinesin motility.
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.
authors.affiliation: Laboratoire d'Enzymologie et Biochimie Structurales, Centre de Recherche de Gif, Centre National de la Recherche Scientifique, Gif sur Yvette, France.
authors.forename: Benoît
authors.initials: B
authors.lastname: Gigant
authors.forename: Weiyi
authors.initials: W
authors.lastname: Wang
authors.forename: Birgit
authors.initials: B
authors.lastname: Dreier
authors.forename: Qiyang
authors.initials: Q
authors.lastname: Jiang
authors.forename: Ludovic
authors.initials: L
authors.lastname: Pecqueur
authors.forename: Andreas
authors.initials: A
authors.lastname: Plückthun
authors.forename: Chunguang
authors.initials: C
authors.lastname: Wang
authors.forename: Marcel
authors.initials: M
authors.lastname: Knossow
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D016880:Anisotropy; D001692:Biological Transport / Q000502:physiology; D003460:Crystallization; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism / Q000502:physiology*; D008958:Models, Molecular; D011487:Protein Conformation; D014404:Tubulin / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: C088547:KTN1 protein, human; D008565:Membrane Proteins; D014404:Tubulin; D000255:Adenosine Triphosphate