3J6H

Nucleotide-free Kinesin motor domain complexed with GMPCPP-microtubule

Summary for 3J6H

• Entry DOI: 10.2210/pdb3j6h/pdb
• EMDB information: 5916
• Descriptor: Tubulin alpha-1A chain, Tubulin beta chain, Kinesin heavy chain isoform 5C, ... (7 entities in total)
• Functional Keywords: kinesin, motor domain, rigor-conformation, nucleotide-free kinesin, microtubule, gmpcpp-microtubule, tubulin, axonal transport, structural protein-motor protein complex, structural protein/motor protein
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 3
• Total formula weight: 137050.57

Authors

Morikawa, M.,Yajima, H.,Nitta, R.,Inoue, S.,Ogura, T.,Sato, C.,Hirokawa, N. (deposition date: 2014-02-21, release date: 2015-04-01, Last modification date: 2024-03-20)

Primary citation

Morikawa, M.,Yajima, H.,Nitta, R.,Inoue, S.,Ogura, T.,Sato, C.,Hirokawa, N.
X-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding
Embo J., 2015

PubMed 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.

PubMed: 25777528
DOI: 10.15252/embj.201490588

Experimental method

ELECTRON MICROSCOPY (8.1 Å)