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PDBsum entry 3j2u
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Motor protein
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PDB id
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3j2u
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Contents |
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309 a.a.
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412 a.a.
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426 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 model for tubulin recognition and deformation by kinesin-13 microtubule depolymerases.
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Authors
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A.B.Asenjo,
C.Chatterjee,
D.Tan,
V.Depaoli,
W.J.Rice,
R.Diaz-Avalos,
M.Silvestry,
H.Sosa.
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Ref.
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Cell Rep, 2013,
3,
759-768.
[DOI no: ]
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PubMed id
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Abstract
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To elucidate the structural basis of the mechanism of microtubule
depolymerization by kinesin-13s, we analyzed complexes of tubulin and the
Drosophila melanogaster kinesin-13 KLP10A by electron microscopy (EM) and
fluorescence polarization microscopy. We report a nanometer-resolution (1.1 nm)
cryo-EM three-dimensional structure of the KLP10A head domain (KLP10AHD) bound
to curved tubulin. We found that binding of KLP10AHD induces a distinct tubulin
configuration with displacement (shear) between tubulin subunits in addition to
curvature. In this configuration, the kinesin-binding site differs from that in
straight tubulin, providing an explanation for the distinct interaction modes of
kinesin-13s with the microtubule lattice or its ends. The KLP10AHD-tubulin
interface comprises three areas of interaction, suggesting a crossbow-type
tubulin-bending mechanism. These areas include the kinesin-13 family conserved
KVD residues, and as predicted from the crossbow model, mutating these residues
changes the orientation and mobility of KLP10AHDs interacting with the
microtubule.
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