 |
PDBsum entry 3x2t
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Motor protein
|
PDB id
|
|
|
|
3x2t
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
X-Ray and cryo-Em structures reveal mutual conformational changes of kinesin and gtp-State microtubules upon binding.
|
|
|
Authors
|
|
M.Morikawa,
H.Yajima,
R.Nitta,
S.Inoue,
T.Ogura,
C.Sato,
N.Hirokawa.
|
|
|
Ref.
|
|
Embo J, 2015,
34,
1270-1286.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The molecular motor kinesin moves along microtubules using energy from ATP
hydrolysis in an initial step coupled with ADP release. In neurons,
kinesin-1/KIF5C preferentially binds to the GTP-state microtubules over
GDP-state microtubules to selectively enter an axon among many processes;
however, because the atomic structure of nucleotide-free KIF5C is unavailable,
its molecular mechanism remains unresolved. Here, the crystal structure of
nucleotide-free KIF5C and the cryo-electron microscopic structure of
nucleotide-free KIF5C complexed with the GTP-state microtubule are presented.
The structures illustrate mutual conformational changes induced by interaction
between the GTP-state microtubule and KIF5C. KIF5C acquires the 'rigor
conformation', where mobile switches I and II are stabilized through L11 and the
initial portion of the neck-linker, facilitating effective ADP release and the
weak-to-strong transition of KIF5C microtubule affinity. Conformational changes
to tubulin strengthen the longitudinal contacts of the GTP-state microtubule in
a similar manner to GDP-taxol microtubules. These results and functional
analyses provide the molecular mechanism of the preferential binding of KIF5C to
GTP-state microtubules.
|
|
|
|
|
|
|
