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Related Experiment Video

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Directly Measuring Forces Within Reconstituted Active Microtubule Bundles

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Published on: May 10, 2022

Force generation in kinesin hinges on cover-neck bundle formation.

Wonmuk Hwang¹, Matthew J Lang, Martin Karplus

¹Department of Biomedical Engineering, Texas A&M University, College Station, TX 77843, USA. hwm@tamu.edu

Structure (London, England : 1993)

|January 11, 2008

Summary

Kinesin motors generate force through a novel mechanism where ATP binding causes the cover strand to form a beta sheet with the neck linker. This cover-neck bundle formation drives kinesin

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Published on: October 15, 2019

Area of Science:

Molecular Biology
Biophysics
Structural Biology

Background:

Kinesin motors are essential for intracellular transport, but the precise mechanism of force generation by ATP binding remains a fundamental question.
Understanding kinesin's force-generating mechanism is crucial for deciphering cellular transport processes and motor protein function.

Purpose of the Study:

To elucidate the molecular mechanism by which ATP binding in kinesin motors generates the force required for processive movement.
To identify the key structural elements responsible for force generation in kinesin.

Main Methods:

Analysis of available kinesin crystal structures.
Molecular dynamics (MD) simulations to model conformational changes.
Comparison of calculated force parameters with experimental force-clamp measurements.

Main Results:

The N-terminal nine-residue cover strand is essential for force generation.
ATP binding induces the cover strand to form a beta sheet with the neck linker (cover-neck bundle).
This cover-neck bundle formation drives neck linker forward motion and subsequent latch-type binding to the motor head.
Calculated stall force and load response align with experimental data.
The proposed mechanism is applicable to multiple kinesin families.

Conclusions:

The formation of the cover-neck bundle upon ATP binding is the primary mechanism for force generation in kinesin motors.
This mechanism explains the efficiency of kinesin as the smallest known processive motor.
The findings provide insights into the fundamental design principles of molecular motors.