A model for the microtubule-Ncd motor protein complex obtained by cryo-electron microscopy and image analysis

Article Abstract:

The atomic structure of the motor domain of Ncd was fitted into three-dimensional density maps of Ncd-microtubule complexes to study the binding of kinesin motors to microtubules. The model shows that Ncd shares an extensive interaction surface with the microtubule and that part of the binding site has loops that contain conserved residues. Furthermore, an intimate contact between the microtubule-bound motor domain and its partner head was observed in the Ncd dimer.

Models, Proteins

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Microtubule interaction site of the kinesin motor

Article Abstract:

A study was conducted on the location of the microtubule-binding site on kinesin. The findings show that microtubule-interacting kinesin residues are found in three loops that cluster in a patch on the motor surface. The critical residues primarily had positive charges. The core of the microtubule-binding interface is located in a highly conserved loop and helix that corresponds topologically to the major actin-binding domain of myosin.

Binding sites (Biochemistry), Active sites (Biochemistry)

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The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain

Article Abstract:

Members of the kinesin superfamily have a similar motor catalytic domain, although they move either to the plus end or the minus end of microtubules. The catalytic domain of kinesin in a dimeric construct, was replaced with the catalytic domain of Ncd, with the result that the motor moves in the kinesin direction. It was demonstrated that the chimera differs from the processive motion of conventional kinesin.

Observations, Catalysts

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