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PDBsum entry 4uxy
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Transport protein
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PDB id
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4uxy
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Contents |
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412 a.a.*
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426 a.a.*
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332 a.a.*
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* C-alpha coords only
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References listed in PDB file
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Key reference
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Title
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Conserved mechanisms of microtubule-Stimulated ADP release, Atp binding, And force generation in transport kinesins.
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Authors
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J.Atherton,
I.Farabella,
I.M.Yu,
S.S.Rosenfeld,
A.Houdusse,
M.Topf,
C.A.Moores.
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Ref.
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Elife, 2014,
3,
e03680.
[DOI no: ]
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PubMed id
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Abstract
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Kinesins are a superfamily of microtubule-based ATP-powered motors, important
for multiple, essential cellular functions. How microtubule binding stimulates
their ATPase and controls force generation is not understood. To address this
fundamental question, we visualized microtubule-bound kinesin-1 and kinesin-3
motor domains at multiple steps in their ATPase cycles--including their
nucleotide-free states--at ∼ 7 Å resolution using cryo-electron microscopy.
In both motors, microtubule binding promotes ordered conformations of conserved
loops that stimulate ADP release, enhance microtubule affinity and prime the
catalytic site for ATP binding. ATP binding causes only small shifts of these
nucleotide-coordinating loops but induces large conformational changes elsewhere
that allow force generation and neck linker docking towards the microtubule plus
end. Family-specific differences across the kinesin-microtubule interface
account for the distinctive properties of each motor. Our data thus provide
evidence for a conserved ATP-driven mechanism for kinesins and reveal the
critical mechanistic contribution of the microtubule interface.
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Headers
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