Crystallographic analysis reveals a unique conformation of the ADP-bound novel rice kinesin K16.
Biochemical studies revealed that the novel rice plant-specific kinesin K16 has several unique enzymatic characteristics as compared to conventional kinesins. The ADP-free form of K16 is very stable, whereas the ADP-free form of conventional kinesins is labile. In the present study, the crystal structure of the novel rice kinesin motor domain (K16MD) complexed with Mg-ADP was determined at 2.4 Å resolutions. The overall structure of K16MD is similar to that of conventional kinesin motor domains, as expected from the high amino acid sequence similarity (43.2%). However, several unique structures in K16 were observed. The position and length of the L5, L11, and L12 loops, which are key functional regions, were different from those observed in conventional kinesins. Moreover, the neck-linker region of the ADP-bound K16MD showed an ordered conformation at a position quite different from that previously observed in conventional kinesins. These structural differences may reflect the unique enzymatic characteristics of rice kinesin K16.
Tanaka
Keiko
K
Division of Bioinformatics, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan.
Umeki
Nobuhisa
N
Mitsui
Toshiaki
T
Fujimoto
Zui
Z
Maruta
Shinsaku
S
D000244:Adenosine Diphosphate / Q000737:chemistry*; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D016547:Kinesins / Q000737:chemistry*; D008969:Molecular Sequence Data; D012275:Oryza / Q000378:metabolism*; D011487:Protein Conformation
D000244:Adenosine Diphosphate; D016547:Kinesins