Switch-based mechanism of kinesin motors

Article Abstract:

Research is presented describing how the KIF1A kinesin motor use hydrolysis of ATP to create force and movement along their linear tracks, known as microtubules. The research combines the use of X-ray crystallography and cryo-electronic microscopy, with the motor in two different functional states.

Microtubules, Cryobiochemistry

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Crystal structure of the kinesin motor domain reveals a structural similarity to myosin

Article Abstract:

Research on microtubule-based motor proteins, using X-ray crystallography, reveals that the human kinesin motor domain and the core of the catalytic domain of the actin-based motor myosin exhibit structural similarities. These two classes of mechanochemical enzymes have a common origin and perform similar force-generating tasks, such as organelle transport and chromosome segregation. A single alpha/beta arrow head-shaped domain with a dimension of 70 x 45 x 45 angstrom composes most of the kinesin motor domain's structure.

Myosin

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Crystal structure of the motor domain of the kinesin-related motor ncd

Article Abstract:

The crystal structure of microtubule-based ATPases of the kinesin superfamily reveals that the ncd and kinesin motor domains have similar structures. X-ray crystallography is used to determine the ncd structure in Drosophila at 2.5 angstrom resolution. These motors share a common microtubule-binding site as is evident from the locations of conserved surface amino acids. A similar method of changing between NTP and NDP state conformations for NTPases is indicated by a comparison of ncd, kinesin, myosin and G proteins.

G proteins

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