5XXV

GDP-microtubule complexed with KIF5C in AMPPNP state

Summary for 5XXV

• Entry DOI: 10.2210/pdb5xxv/pdb
• Related: 5XXT 5XXW 5XXX
• EMDB information: 6779 6781 6782 6783
• Descriptor: Tubulin alpha-1A chain, Tubulin beta chain, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: microtubule, kif5c, kinesin, structural protein
• Biological source: Sus scrofa (Pig); More
• Total number of polymer chains: 18
• Total formula weight: 876953.03

Authors

Morikawa, M.,Shigematsu, H.,Nitta, R.,Hirokawa, N. (deposition date: 2017-07-05, release date: 2018-10-10, Last modification date: 2019-11-06)

Primary citation

Shima, T.,Morikawa, M.,Kaneshiro, J.,Kambara, T.,Kamimura, S.,Yagi, T.,Iwamoto, H.,Uemura, S.,Shigematsu, H.,Shirouzu, M.,Ichimura, T.,Watanabe, T.M.,Nitta, R.,Okada, Y.,Hirokawa, N.
Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport
J. Cell Biol., 217:4164-4183, 2018

PubMed Abstract: Kinesin-1, the founding member of the kinesin superfamily of proteins, is known to use only a subset of microtubules for transport in living cells. This biased use of microtubules is proposed as the guidance cue for polarized transport in neurons, but the underlying mechanisms are still poorly understood. Here, we report that kinesin-1 binding changes the microtubule lattice and promotes further kinesin-1 binding. This high-affinity state requires the binding of kinesin-1 in the nucleotide-free state. Microtubules return to the initial low-affinity state by washing out the binding kinesin-1 or by the binding of non-hydrolyzable ATP analogue AMPPNP to kinesin-1. X-ray fiber diffraction, fluorescence speckle microscopy, and second-harmonic generation microscopy, as well as cryo-EM, collectively demonstrated that the binding of nucleotide-free kinesin-1 to GDP microtubules changes the conformation of the GDP microtubule to a conformation resembling the GTP microtubule.

PubMed: 30297389
DOI: 10.1083/jcb.201711178

Experimental method

ELECTRON MICROSCOPY (6.46 Å)