How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1.

Jingyu Qin,Hui Zhang,Yizhao Geng,Qing Ji

doi:10.3390/ijms21186977

Abstract

Kinesin-1 is a typical motile molecular motor and the founding member of the kinesin family. The most significant feature in the unidirectional motion of kinesin-1 is its processivity. To realize the fast and processive movement on the microtubule lattice, kinesin-1 efficiently transforms the chemical energy of nucleotide binding and hydrolysis to the energy of mechanical movement. The chemical and mechanical cycle of kinesin-1 are coupled to avoid futile nucleotide hydrolysis. In this paper, the research on the mechanical pathway of energy transition and the regulating mechanism of the mechanochemical cycle of kinesin-1 is reviewed.

Highlights

Kinesin is a molecular walking motor protein inside cells
The entrance of the ATP molecule into the nucleotide-binding pocket can induce a series of conformational changes of the pocket, which can be amplified and transmitted to the neck linker portion to initiate the docking movement of neck linker to the motor domain [12,34,35,36,37,38,39,40,41,42]
The neck linker of kinesin-1 consists of 14 residues and can be divided into three parts according to their different conformational changes in the docking movement

Summary

Introduction

Kinesin is a molecular walking motor protein inside cells. The size of kinesin is smaller than the other two members of motor proteins, myosin and dynein. The conformational changes of the neck linker in different nucleotide-binding states are the key processes in the walking movement of kinesin-1 [9,10,11,12,13]. The entire structure of nucleotide-binding pocket of kinesin-1 is a perfect match for ATP molecules in both geometry and interaction (Figure 2).

Results

Conclusion