PDBsum entry 5xxx

Structural protein

PDB id: 5xxx

Contents

Protein chains

(+ 3 more) 428 a.a.

(+ 3 more) 426 a.a.

Ligands

GTP ×9

G2P ×9

Metals

_MG ×18

Waters ×36

PDB id:

5xxx

Name:

Structural protein

Title:

Gmpcpp-microtubule complexed with nucleotide-free kif5c

Structure:

Tubulin alpha-1a chain. Chain: a, c, e, g, i, k, m, o, q. Fragment: unp residues 2-439. Synonym: alpha-tubulin 1,tubulin alpha-1 chain. Tubulin beta chain. Chain: b, d, f, h, j, l, n, p, r. Fragment: unp residues 2-427. Synonym: beta-tubulin

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Organism_taxid: 9823

Authors:

M.Morikawa,H.Shigematsu,R.Nitta,N.Hirokawa

Key ref:

T.Shima et al. (2018). Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport. J Cell Biol, 217, 4164-4183. PubMed id: 30297389

Date:

05-Jul-17 Release date: 10-Oct-18

Protein chains

P02550  (TBA1A_PIG) -  Tubulin alpha-1A chain from Sus scrofa

Seq: 451 a.a.

Struc: 428 a.a.*

Protein chains

P02554  (TBB_PIG) -  Tubulin beta chain from Sus scrofa

Seq: 445 a.a.

Struc: 426 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains A, C, E, G, I, K, M, O, Q: E.C.3.6.5.- - ?????

J Cell Biol 217:4164-4183 (2018)

PubMed id: 30297389

Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport.

T.Shima, M.Morikawa, J.Kaneshiro, T.Kambara, S.Kamimura, T.Yagi, H.Iwamoto, S.Uemura, H.Shigematsu, M.Shirouzu, T.Ichimura, T.M.Watanabe, R.Nitta, Y.Okada, N.Hirokawa.

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.