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PDBsum entry 3j8x
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Motor protein/structural protein
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PDB id
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3j8x
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Contents |
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316 a.a.
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430 a.a.
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431 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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High-Resolution structures of kinesin on microtubules provide a basis for nucleotide-Gated force-Generation.
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Authors
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Z.Shang,
K.Zhou,
C.Xu,
R.Csencsits,
J.C.Cochran,
C.V.Sindelar.
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Ref.
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Elife, 2014,
3,
e04686.
[DOI no: ]
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PubMed id
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Abstract
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Microtubule-based transport by the kinesin motors, powered by ATP hydrolysis, is
essential for a wide range of vital processes in eukaryotes. We obtained insight
into this process by developing atomic models for no-nucleotide and ATP states
of the monomeric kinesin motor domain on microtubules from cryo-EM
reconstructions at 5-6 Å resolution. By comparing these models with existing
X-ray structures of ADP-bound kinesin, we infer a mechanistic scheme in which
microtubule attachment, mediated by a universally conserved 'linchpin' residue
in kinesin (N255), triggers a clamshell opening of the nucleotide cleft and
accompanying release of ADP. Binding of ATP re-closes the cleft in a manner that
tightly couples to translocation of cargo, via kinesin's 'neck linker' element.
These structural transitions are reminiscent of the analogous
nucleotide-exchange steps in the myosin and F1-ATPase motors and inform how the
two heads of a kinesin dimer 'gate' each other to promote coordinated stepping
along microtubules.
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