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

Author

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  • Ruifang Guan

    (MOE Key Laboratory of Protein Science, Tsinghua University
    School of Life 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
    School of Life Science, Tsinghua University)

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.

Suggested Citation

  • Ruifang Guan & Lei Zhang & Qian Peter Su & Keith J. Mickolajczyk & Geng-Yuan Chen & William O. Hancock & Yujie Sun & Yongfang Zhao & Zhucheng Chen, 2017. "Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin," Nature Communications, Nature, vol. 8(1), pages 1-9, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14951
    DOI: 10.1038/ncomms14951
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