Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.
Journal, issue, pages	Sci Rep, Vol. 16, Issue 1, Page 487, Year 2026
Publish date	Jan 5, 2026
Authors	Satoki Shibata / Matthew Y Wang / Tsuyoshi Imasaki / Hideki Shigematsu / Diego Ugarte La Torre / Yuanyuan Wei / Chacko Jobichen / Hajime Hagio / J Sivaraman / Yuji Sugita / Sharyn A Endow / Ryo Nitta /
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 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. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1038/s41598-025-28573-7.
External links	Sci Rep / PubMed:41491787 / PubMed Central
Methods	EM (helical sym.) / X-ray diffraction
Resolution	3.15 - 4.02 Å
Structure data	39664 8yy2 EMDB-39664, PDB-8yy2: Kinesin-14 in nucleotide-free state bound to 13 PF Microtubule Method: EM (helical sym.) / Resolution: 3.6 Å 39665 8yy3 EMDB-39665, PDB-8yy3: Kinesin-14 in nucleotide-free state bound to 14 PF Microtubule Method: EM (helical sym.) / Resolution: 3.24 Å 39666 8yy4 EMDB-39666, PDB-8yy4: Kinesin-14 with AlF3 bound to 13 PF Microtubule Method: EM (helical sym.) / Resolution: 4.02 Å 39667 8yy5 EMDB-39667, PDB-8yy5: Kinesin-14 with AlF3 bound to 14 PF Microtubule Method: EM (helical sym.) / Resolution: 3.99 Å PDB-8yue: Crystal structure of the kinesin-14 motor protein from Drosophila melanogaster Method: X-RAY DIFFRACTION / Resolution: 3.15 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-PO4: PHOSPHATE ION ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying moleculeYM ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-ALF*: TETRAFLUOROALUMINATE ION
Source	sus scrofa (pig) drosophila melanogaster (fruit fly)
Keywords	MOTOR PROTEIN / Kinesin-related / Microtubule motor protein / Spindle motor / CELL CYCLE / Kinesin Motor Proteins / Force Production / Power Stroke Fluctuations / Motor Spring-like Element / Reversed Motility / Mechanochemical Coupling / Mechanical States