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Biophys J. 2011 Sep 7;101(5):1105-13. doi: 10.1016/j.bpj.2011.07.017.

Hysteresis-based mechanism for the directed motility of the Ncd motor.

Author information

1
Department of Biomedical Engineering, Texas A&M University, College Station, Texas, USA.

Abstract

Ncd is a Kinesin-14 family protein that walks to the microtubule's minus end. Although available structures show its α-helical neck in either pre- or post-stroke orientations, little is known about the transition between these two states. Using a combination of molecular dynamics simulations and structural analyses, we find that the neck sequentially makes intermediate contacts with the motor head along its mostly longitudinal path, and it develops a 24° twist in the post-stroke orientation. The forward (pre-stroke to post-stroke) motion has an ∼4.5 k(B)T (where k(B) is the Boltzmann constant, and T=300 K) free-energy barrier and is a diffusion guided by the intermediate contacts. The post-stroke free-energy minimum is higher and is formed ∼10° before reaching the orientation in the post-stroke crystal structure, consistent with previous structural data. The importance of intermediate contacts correlates with the existing motility data, including those for mutant Ncds. Unlike the forward motion, the recovery stroke goes nearly downhill in free energy, powered in part by torsional relaxation of the neck. The hysteresis in the energetics of the neck motion arises from the mechanical compliance of the protein, and together with guided diffusion, it may be key to the directed motility of Ncd.

PMID:
21889447
PMCID:
PMC3164182
DOI:
10.1016/j.bpj.2011.07.017
[Indexed for MEDLINE]
Free PMC Article

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