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PDBsum entry 4ozq
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Motor protein
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PDB id
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4ozq
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PDB id:
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| Name: |
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Motor protein
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Title:
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Crystal structure of the mouse kif14 motor domain
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Structure:
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Chimera of maltose-binding periplasmic protein and kinesin family member 14 protein. Chain: a, b. Engineered: yes
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Source:
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Escherichia coli umea 3304-1, mus musculus. Mouse. Organism_taxid: 1281237, 10090. Gene: g962_03763, kif14,kif14. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.71Å
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R-factor:
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0.266
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R-free:
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0.308
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Authors:
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K.Arora,L.Talje,A.B.Asenjo,P.Andersen,K.Atchia,M.Joshi,H.Sosa, B.H.Kwok,J.S.Allingham
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Key ref:
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K.Arora
et al.
(2014).
KIF14 binds tightly to microtubules and adopts a rigor-like conformation.
J Mol Biol,
426,
2997-3015.
PubMed id:
DOI:
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Date:
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18-Feb-14
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Release date:
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09-Jul-14
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PROCHECK
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Headers
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References
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L0N7N1
(KIF14_MOUSE) -
Kinesin-like protein KIF14 from Mus musculus
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Seq:
Struc:
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1674 a.a.
683 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 342 residue positions (black
crosses)
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DOI no:
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J Mol Biol
426:2997-3015
(2014)
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PubMed id:
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KIF14 binds tightly to microtubules and adopts a rigor-like conformation.
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K.Arora,
L.Talje,
A.B.Asenjo,
P.Andersen,
K.Atchia,
M.Joshi,
H.Sosa,
J.S.Allingham,
B.H.Kwok.
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ABSTRACT
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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.
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Links
