Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin

Ruifang Guan, Lei Zhang, Qian Peter Su, Keith J. Mickolajczyk, Geng-Yuan Chen, William O. Hancock, Yujie Sun, Yongfang Zhao and Zhucheng Chen ()
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Ruifang Guan: MOE Key Laboratory of Protein Science, Tsinghua University
Lei Zhang: National Laboratory of Biomacromolecules, Institute of Biophysics
Qian Peter Su: State Key Laboratory of Membrane Biology, Biodynamic Optical Imaging Center (BIOPIC), School of Life Sciences, Peking University
Keith J. Mickolajczyk: Pennsylvania State University, University Park, Pennsylvania 16802, USA
Geng-Yuan Chen: Pennsylvania State University, University Park, Pennsylvania 16802, USA
William O. Hancock: Pennsylvania State University, University Park, Pennsylvania 16802, USA
Yujie Sun: State Key Laboratory of Membrane Biology, Biodynamic Optical Imaging Center (BIOPIC), School of Life Sciences, Peking University
Yongfang Zhao: National Laboratory of Biomacromolecules, Institute of Biophysics
Zhucheng Chen: MOE Key Laboratory of Protein Science, Tsinghua University

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: Abstract Kinesins hydrolyse ATP to transport intracellular cargoes along microtubules. Kinesin neck linker (NL) functions as the central mechano-chemical coupling element by changing its conformation through the ATPase cycle. Here we report the crystal structure of kinesin-6 Zen4 in a nucleotide-free, apo state, with the NL initial segment (NIS) adopting a backward-docked conformation and the preceding α6 helix partially melted. Single-molecule fluorescence resonance energy transfer (smFRET) analyses indicate the NIS of kinesin-1 undergoes similar conformational changes under tension in the two-head bound (2HB) state, whereas it is largely disordered without tension. The backward-docked structure of NIS is essential for motility of the motor. Our findings reveal a key missing conformation of kinesins, which provides the structural basis of the stable 2HB state and offers a tension-based rationale for an optimal NL length to ensure processivity of the motor.

Date: 2017
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DOI: 10.1038/ncomms14951

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