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PDBsum entry 5hnx
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Structural protein/motor protein
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PDB id
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5hnx
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Contents |
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412 a.a.
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426 a.a.
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320 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural basis of backwards motion in kinesin-1-Kinesin-14 chimera: implication for kinesin-14 motility.
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Authors
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M.Yamagishi,
H.Shigematsu,
T.Yokoyama,
M.Kikkawa,
M.Sugawa,
M.Aoki,
M.Shirouzu,
J.Yajima,
R.Nitta.
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Ref.
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Structure, 2016,
24,
1322-1334.
[DOI no: ]
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PubMed id
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Abstract
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Kinesin-14 is a unique minus-end-directed microtubule-based motor. A swinging
motion of a class-specific N-terminal neck helix has been proposed to produce
minus-end directionality. However, it is unclear how swinging of the neck helix
is driven by ATP hydrolysis utilizing the highly conserved catalytic core among
all kinesins. Here, using a motility assay, we show that in addition to the neck
helix, the conserved five residues at the C-terminal region in kinesin-14,
namely the neck mimic, are necessary to give kinesin-1 an ability to reverse its
directionality toward the minus end of microtubules. Our structural analyses
further demonstrate that the C-terminal neck mimic, in cooperation with
conformational changes in the catalytic core during ATP binding, forms a
kinesin-14 bundle with the N-terminal neck helix to swing toward the minus end
of microtubules. Thus, the neck mimic plays a crucial role in coupling the
chemical ATPase reaction with the mechanical cycle to produce the
minus-end-directed motility of kinesin-14.
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