EC Number   |
Reference |
|---|
   3.6.4.B1 | crystallized at 4°C using sitting drop vapor diffusion method and 20% polyethylene glycol 3350 in 0.2 M disodium hydrogen phosphate, 2.3 A resolution |
669229 |
| 3.6.4.B1 | four structures of the fragment encoding the potato KCBP from amino acids 884-1252, which include the motor core and the C-terminal extension containing the calmodulin-binding motif. The kinesin motor is in the ATP-like conformation, but loop 11 exhibits different conformational states, both ordered and disordered. When structured, loop 11 adds three additional helical turns to the N-terminal part of the following helix alpha4. Positioning of the calmodulin binding helix is not decided by crystal packing forces but is determined by the conformational state of the motor |
688699 |
| 3.6.4.B1 | 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 |
711116 |
