Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation

Chunting Zhang, Changmiao Guo, Ryan W. Russell, Caitlin M. Quinn, Mingyue Li, John C. Williams (), Angela M. Gronenborn () and Tatyana Polenova ()
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Chunting Zhang: University of Delaware
Changmiao Guo: University of Delaware
Ryan W. Russell: University of Delaware
Caitlin M. Quinn: University of Delaware
Mingyue Li: University of Delaware
John C. Williams: Beckman Research Institute of City of Hope
Angela M. Gronenborn: University of Pittsburgh School of Medicine
Tatyana Polenova: University of Delaware

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract Microtubules (MTs) and their associated proteins play essential roles in maintaining cell structure, organelle transport, cell motility, and cell division. Two motors, kinesin and cytoplasmic dynein link the MT network to transported cargos using ATP for force generation. Here, we report an all-atom NMR structure of nucleotide-free kinesin-1 motor domain (apo-KIF5B) in complex with paclitaxel-stabilized microtubules using magic-angle-spinning (MAS) NMR spectroscopy. The structure reveals the position and orientation of the functionally important neck linker and how ADP induces structural and dynamic changes that ensue in the neck linker. These results demonstrate that the neck linker is in the undocked conformation and oriented in the direction opposite to the KIF5B movement. Chemical shift perturbations and intensity changes indicate that a significant portion of ADP-KIF5B is in the neck linker docked state. This study also highlights the unique capability of MAS NMR to provide atomic-level information on dynamic regions of biological assemblies.

Date: 2022
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DOI: 10.1038/s41467-022-34026-w

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