8YUE

Crystal structure of the kinesin-14 motor protein from Drosophila melanogaster

Summary for 8YUE

• Entry DOI: 10.2210/pdb8yue/pdb
• Descriptor: Protein claret segregational, ADENOSINE-5'-DIPHOSPHATE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: kinesin-related, microtubule motor protein, spindle motor, motor protein
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 2
• Total formula weight: 90147.17

Authors

Wei, Y.,Jobichen, C.,Imasaki, T.,Nitta, R.,Wang, M.Y.,Sivaraman, J.,Endow, S.A. (deposition date: 2024-03-27, release date: 2025-04-09, Last modification date: 2026-04-22)

Primary citation

Shibata, S.,Wang, M.Y.,Imasaki, T.,Shigematsu, H.,Ugarte La Torre, D.,Wei, Y.,Jobichen, C.,Hagio, H.,Sivaraman, J.,Sugita, Y.,Endow, S.A.,Nitta, R.
Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.
Sci Rep, 16:487-487, 2026

PubMed Abstract: Kinesin motors use ATP to produce force in cells, yet the conformational changes that generate force remain uncertain. Here, we report structural and mechanistic insights into a minus-end-directed kinesin-14 that exhibits increased mechanical output – the variant motor binds microtubules more tightly and moves with faster velocity than wild type. High-resolution structures, together with molecular dynamics simulations, reveal previously unobserved transitions in the nucleotide hydrolysis cycle. ADP release, triggered by microtubule binding, is coupled to twisting of the central β-sheet and stabilization of the stalk prior to the power stroke. ATP binding induces stalk fluctuations and a swing of the neck mimic, an element analogous to the kinesin-1 neck linker, resembling neck linker docking in plus-end-directed kinesins. The power stroke, characterized by a large stalk rotation, is followed by motor detachment from microtubules. The subsequent recovery stroke occurs while the motor is bound to ADP and free Pi, accompanied by β-strand-to-loop transitions, or β-sheet melting, implying that β-sheet refolding facilitates Pi release. The observed twisting and melting identify the central β-sheet as the long-sought elastic element or spring required for motor force production. The transitions we observe in kinesin-14 may also apply to other kinesins – this remains to be tested.

PubMed: 41491787
DOI: 10.1038/s41598-025-28573-7

Experimental method

X-RAY DIFFRACTION (3.15 Å)