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4OZQ

Crystal structure of the mouse Kif14 motor domain

Summary for 4OZQ
Entry DOI10.2210/pdb4ozq/pdb
DescriptorChimera of Maltose-binding periplasmic protein and Kinesin family member 14 protein, ADENOSINE-5'-DIPHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordskinesin, atpase, motor protein
Biological sourceEscherichia coli UMEA 3304-1
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Total number of polymer chains2
Total formula weight159929.88
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 citationArora, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.71 Å)
Structure validation

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