4OZQ

Crystal structure of the mouse Kif14 motor domain

Summary for 4OZQ

• Entry DOI: 10.2210/pdb4ozq/pdb
• Descriptor: Chimera of Maltose-binding periplasmic protein and Kinesin family member 14 protein, ADENOSINE-5'-DIPHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: kinesin, atpase, motor protein
• Biological source: Escherichia coli UMEA 3304-1; More
• Total number of polymer chains: 2
• Total formula weight: 159929.88

Authors

Arora, K.,Talje, L.,Asenjo, A.B.,Andersen, P.,Atchia, K.,Joshi, M.,Sosa, H.,Kwok, B.H.,Allingham, J.S. (deposition date: 2014-02-18, release date: 2014-07-09, Last modification date: 2023-12-27)

Primary citation

Arora, K.,Talje, L.,Asenjo, A.B.,Andersen, P.,Atchia, K.,Joshi, M.,Sosa, H.,Allingham, J.S.,Kwok, B.H.
KIF14 binds tightly to microtubules and adopts a rigor-like conformation.
J.Mol.Biol., 426:2997-3015, 2014

PubMed Abstract: The mitotic kinesin motor protein KIF14 is essential for cytokinesis during cell division and has been implicated in cerebral development and a variety of human cancers. Here we show that the mouse KIF14 motor domain binds tightly to microtubules and does not display typical nucleotide-dependent changes in this affinity. It also has robust ATPase activity but very slow motility. A crystal structure of the ADP-bound form of the KIF14 motor domain reveals a dramatically opened ATP-binding pocket, as if ready to exchange its bound ADP for Mg·ATP. In this state, the central β-sheet is twisted ~10° beyond the maximal amount observed in other kinesins. This configuration has only been seen in the nucleotide-free states of myosins-known as the "rigor-like" state. Fitting of this atomic model to electron density maps from cryo-electron microscopy indicates a distinct binding configuration of the motor domain to microtubules. We postulate that these properties of KIF14 are well suited for stabilizing midbody microtubules during cytokinesis.

PubMed: 24949858
DOI: 10.1016/j.jmb.2014.05.030

Experimental method

X-RAY DIFFRACTION (2.71 Å)