Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement

Jinqi Ren; Yong Zhang; Shuang Wang; Lin Huo; Jizhong Lou; Wei Feng

doi:10.1016/j.jmb.2018.05.010

Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement

J Mol Biol. 2018 Jul 6;430(14):2030-2041. doi: 10.1016/j.jmb.2018.05.010. Epub 2018 May 9.

Authors

Jinqi Ren¹, Yong Zhang², Shuang Wang³, Lin Huo¹, Jizhong Lou⁴, Wei Feng⁵

Affiliations

¹ National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.
² Key Laboratory of RNA Biology, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.
³ National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
⁴ Key Laboratory of RNA Biology, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
⁵ National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China. Electronic address: wfeng@ibp.ac.cn.

PMID: 29752968
DOI: 10.1016/j.jmb.2018.05.010

Abstract

Processive kinesin motors contain a neck linker (NL) that mediates the chemo-mechanical coupling and controls the directionality and processivity. However, kinesin-3 NL remains poorly determined due to the lack of the structural information of the junction with the following neck coil (NC). Here, we determined the structure of the motor domain (MD)-NL-NC_NT tandem of KIF13B that defines the junction between NL and NC and delineates kinesin-3 NL. Unexpectedly, the length of kinesin-3 NL is much shorter than the previously predicted one. In the MD-NL-NC_NT structure, NL docks onto the MD with a conventional mode but the interaction between NL and the MD is relatively weak due to the shorter N-terminal cover strand of the MD. The optimal short NL and its weak interaction with the MD would generate the tight inter-head strain and facilitate the NL undocking, which may contribute to the fast and superprocessive motility of kinesin-3.

Keywords: X-ray crystallography; interaction; intracellular transport; molecular dynamics simulation; molecular motor.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Motifs
Humans
Kinesins / chemistry*
Models, Molecular
Molecular Dynamics Simulation
Multigene Family
Protein Conformation

Substances

Kinesins