Abstract
Recently, we have successfully dissolved the crystal structure of ADP bound K16 motor domain. The overall structure of the K16MD is similar to that of conventional kinesin motor domains, as expected from the high similarity of amino acid sequence. However, neck-linker region of K16 showed an ordered conformation in a position like that of Eg5. Previously, we have designed the K16 motor domain chimera protein fused with GFP at the neck-linker in order to monitor the conformational change of the neck-linker during ATP hydrolysis by small angle X-ray solution scattering.
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