Shaft Function of Kinesin-1's α4 Helix in the Processive Movement.

ABSTRACT:

Introduction

Kinesin-1 motor is a molecular walking machine constructed with amino acids. The understanding of how those structural elements play their mechanical roles is the key to the understanding of kinesin-1 mechanism.

Methods

Using molecular dynamics simulations, we investigate the role of a helix structure, α4 (also called switch-II helix), of kinesin-1's motor domain in its processive movement along microtubule.

Results

Through the analysis of the structure and the interactions between α4 and the surrounding residues in different nucleotide-binding states, we find that, mechanically, this helix functions as a shaft for kinesin-1's motor-domain rotation and, structurally, it is an amphipathic helix ensuring its shaft functioning. The hydrophobic side of α4 con

SUBMITTER: Ma YL 

PROVIDER: S-EPMC6816713 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature