5HNY

Structural basis of backwards motion in kinesin-14: plus-end directed nKn669 in the AMPPNP state

Summary for 5HNY

• Entry DOI: 10.2210/pdb5hny/pdb
• Related: 5HNW 5HNX 5HNZ
• EMDB information: 8058 8060
• Descriptor: Tubulin alpha-1B chain, Tubulin beta-2B chain, Protein claret segregational, Kinesin-1/Kinesin-14, Protein claret segregational, ... (8 entities in total)
• Functional Keywords: kinesin, kinesin-14, microtubule, atpase, structural protein-motor protein complex, structural protein/motor protein
• Biological source: Drosophila melanogaster (Fruit fly); More
• Cellular location: Cytoplasm, cytoskeleton: P81947 Q6B856 P20480
• Total number of polymer chains: 3
• Total formula weight: 140544.05

Authors

Shigematsu, H.,Yokoyama, T.,Kikkawa, M.,Shirouzu, M.,Nitta, R. (deposition date: 2016-01-19, release date: 2016-08-10, Last modification date: 2024-10-23)

Primary citation

Yamagishi, M.,Shigematsu, H.,Yokoyama, T.,Kikkawa, M.,Sugawa, M.,Aoki, M.,Shirouzu, M.,Yajima, J.,Nitta, R.
Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication for Kinesin-14 Motility
Structure, 24:1322-1334, 2016

PubMed Abstract: Kinesin-14 is a unique minus-end-directed microtubule-based motor. A swinging motion of a class-specific N-terminal neck helix has been proposed to produce minus-end directionality. However, it is unclear how swinging of the neck helix is driven by ATP hydrolysis utilizing the highly conserved catalytic core among all kinesins. Here, using a motility assay, we show that in addition to the neck helix, the conserved five residues at the C-terminal region in kinesin-14, namely the neck mimic, are necessary to give kinesin-1 an ability to reverse its directionality toward the minus end of microtubules. Our structural analyses further demonstrate that the C-terminal neck mimic, in cooperation with conformational changes in the catalytic core during ATP binding, forms a kinesin-14 bundle with the N-terminal neck helix to swing toward the minus end of microtubules. Thus, the neck mimic plays a crucial role in coupling the chemical ATPase reaction with the mechanical cycle to produce the minus-end-directed motility of kinesin-14.

PubMed: 27452403
DOI: 10.1016/j.str.2016.05.021

Experimental method

ELECTRON MICROSCOPY (6.3 Å)