PDBsum entry 3wrd

Motor protein

PDB id: 3wrd

Contents

Protein chains

310 a.a.

Ligands

SO4 ×2

Waters ×5

PDB id:

3wrd

Name:

Motor protein

Title:

Crystal structure of the kif5c motor domain without any nucleotide

Structure:

Kinesin heavy chain isoform 5c. Chain: a, b. Fragment: motor domain, residues 1-334. Synonym: kinesin heavy chain neuron-specific 2. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: kif5c. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.86Å R-factor: 0.241 R-free: 0.299

Authors:

S.Inoue,R.Nitta,N.Hirokawa

Key ref:

M.Morikawa et al. (2015). X-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding. Embo J, 34, 1270-1286. PubMed id: 25777528 DOI: 10.15252/embj.201490588

Date:

21-Feb-14 Release date: 01-Apr-15

Protein chains

P28738  (KIF5C_MOUSE) -  Kinesin heavy chain isoform 5C from Mus musculus

Seq: 956 a.a.

Struc: 310 a.a.

Enzyme reactions

• Enzyme class: E.C.3.6.4.- - ?????

DOI no: 10.15252/embj.201490588

Embo J 34:1270-1286 (2015)

PubMed id: 25777528

X-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding.

M.Morikawa, H.Yajima, R.Nitta, S.Inoue, T.Ogura, C.Sato, N.Hirokawa.

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.