The crystal structure of dimeric kinesin and implications for microtubule-dependent motility.
The dimeric form of the kinesin motor and neck domain from rat brain with bound ADP has been solved by X-ray crystallography. The two heads of the dimer are connected via a coiled-coil alpha-helical interaction of their necks. They are broadly similar to one another; differences are most apparent in the head-neck junction and in a moderate reorientation of the neck helices in order to adopt to the coiled-coil conformation. The heads show a rotational symmetry (approximately 120 degrees) about an axis close to that of the coiled-coil. This arrangement is unexpected since it is not compatible with the microtubule lattice. In this arrangement, the two heads of a kinesin dimer could not have equivalent interactions with microtubules.
Kozielski
F
F
Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany.
Sack
S
S
Marx
A
A
Thormählen
M
M
Schönbrunn
E
E
Biou
V
V
Thompson
A
A
Mandelkow
E M
EM
Mandelkow
E
E
D000244:Adenosine Diphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D019281:Dimerization; D016547:Kinesins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D051381:Rats
D000244:Adenosine Diphosphate; D016547:Kinesins