5XXX
GMPCPP-microtubule complexed with nucleotide-free KIF5C
Summary for 5XXX
| Entry DOI | 10.2210/pdb5xxx/pdb |
| Related | 5XXT 5XXV 5XXW |
| EMDB information | 6779 6781 6782 6783 |
| Descriptor | Tubulin alpha-1A chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (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 | 877873.83 |
| 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 Cited by 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: 30297389DOI: 10.1083/jcb.201711178 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.43 Å) |
Structure validation
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