Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli BL21(DE3)pLys strain | Oryza sativa |
Crystallization (Comment) | Organism |
---|---|
K16MD, the rice kinesin motor domain complexed with Mg-ADP is crystallized by the sitting drop vapor diffusion method at 19.85°C, resulting in a 2.4 A resolution. The ADP-free form of the novel rice-plant-specific kinesin K16 is very stable, whereas the ADP-free form of conventional kinesins is labile. The overall structure of K16MD is similar to that of conventional kinesin motors domains, as expected from the high amino acid sequence similarity of 43.2%. The position and length of the L5, L11m and L12 loops, which are key functional regions, are different from those observed in conventional kinesins. Moreover, the neck-lonker region of the ADP-bound K16MD shows an ordered confirmation at a position quite different from that of conventional kinesins | Oryza sativa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryza sativa | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
K16MD | - |
Oryza sativa |
kinesin K-16 | novel rice-plant-specific kinesin K16 | Oryza sativa |
kinesin K16MD | - |
Oryza sativa |