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PDBsum entry 1n6m
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, Ncd.
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Authors
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M.Yun,
C.E.Bronner,
C.G.Park,
S.S.Cha,
H.W.Park,
S.A.Endow.
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Ref.
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Embo J, 2003,
22,
5382-5389.
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PubMed id
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Abstract
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Molecular motors undergo conformational changes to produce force and move along
cytoskeletal filaments. Structural changes have been detected in kinesin motors;
however, further changes are expected because previous crystal structures are in
the same or closely related conformations. We report here a 2.5 A crystal
structure of the minus-end kinesin, Ncd, with the coiled-coil stalk/neck and one
head rotated by approximately 75 degrees relative to the other head. The two
heads are asymmetrically positioned with respect to the stalk and show asymmetry
of nucleotide state: one head is fully occupied, but the other is unstably bound
to ADP. Unlike previous structures, our new atomic model can be fit into
cryoelectron microscopy density maps of the motor attached to microtubules,
where it appears to resemble a one-head-bound motor with the stalk rotated
towards the minus end. Interactions between neck and motor core residues,
observed in the head that moves with the stalk, are disrupted in the other head,
permitting rotation of the stalk/neck. The rotation could represent a
force-producing stroke that directs the motor to the minus end.
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