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Three-dimensional structure of motor molecules.

K Hirose1, L A Amos

  • 1National Institute for Advanced Interdisciplinary Research, Tsukuba, Ibaraki, Japan. khirose@nair.go.jp

Cellular and Molecular Life Sciences : CMLS
|February 24, 2001
PubMed
Summary

Motor proteins kinesin and ncd bind microtubules similarly, but their differing head positions suggest distinct movement mechanisms. Structural similarities to myosin indicate shared motor protein evolution.

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Area of Science:

  • Molecular and Cellular Biology
  • Biophysics
  • Structural Biology

Background:

  • Motor proteins are essential for intracellular transport, utilizing ATP hydrolysis to generate force and movement along cytoskeletal filaments.
  • Kinesin and its related protein ncd are microtubule-based motor proteins with distinct directional properties.
  • Myosin, another major motor protein family, interacts with actin filaments and shares structural homology with kinesins.

Purpose of the Study:

  • To elucidate the three-dimensional structural interactions of kinesin and ncd motor proteins with microtubules at the molecular level.
  • To compare the binding modes and structural features of kinesin, ncd, and myosin to understand conserved and divergent motor protein mechanisms.
  • To investigate the structural basis for the different kinetic properties and movement strategies of these motor proteins.

Main Methods:

  • Analysis of three-dimensional structures derived from electron micrographs of microtubules decorated with motor proteins.
  • X-ray crystallography to determine the atomic resolution structures of kinesin and ncd.
  • Comparative structural analysis of kinesin, ncd, and myosin.

Main Results:

  • Both kinesin and ncd motor domains bind to tubulin in a similar manner, primarily through one of their two heads.
  • A notable difference in the positioning of the second head between kinesin and ncd was observed, correlating with their opposite directions of movement.
  • X-ray crystallography revealed high structural similarity between kinesin and ncd at atomic resolution, indicating homology with myosin.

Conclusions:

  • Kinesin and ncd likely share common evolutionary origins and fundamental binding mechanisms with myosin.
  • Despite structural similarities, kinesin and ncd exhibit distinct kinetic properties and movement mechanisms compared to myosin.
  • Kinesin and ncd may employ biased diffusion rather than a lever-arm-like amplification mechanism for microtubule translocation.

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