Structure of the complex of a mitotic kinesin with its calcium binding regulator

Much of the transport, tension, and movement in mitosis depends on kinesins, the ATP-powered microtubule-based motors. We report the crystal structure of a kinesin complex, the mitotic kinesin KCBP bound to its principal regulator KIC. Shown to be a Ca²⁺ sensor, KIC works as an allosteric trap. Exte...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2009-05, Vol.106 (20), p.8175-8179
Main Authors: Vinogradova, Maia V, Malanina, Galina G, Reddy, Anireddy S.N, Fletterick, Robert J
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Amino acids
Arabidopsis Proteins - chemistry
Biological Sciences
Calcium
Calcium-Binding Proteins - chemistry
Calmodulin binding proteins
Calmodulin-Binding Proteins - chemistry
Cell division
Crystal structure
Crystallography, X-Ray
Hydrolysis
Kinesin - chemistry
Microtubule-Associated Proteins - chemistry
Microtubules
Mitosis
Molecular structure
Motors
Nucleotides
Physiological regulation
Protein Binding
Protein Conformation
Proteins
Sensors
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Summary:Much of the transport, tension, and movement in mitosis depends on kinesins, the ATP-powered microtubule-based motors. We report the crystal structure of a kinesin complex, the mitotic kinesin KCBP bound to its principal regulator KIC. Shown to be a Ca²⁺ sensor, KIC works as an allosteric trap. Extensive intermolecular interactions with KIC stabilize kinesin in its ADP-bound conformation. A critical component of the kinesin motile mechanism, called the neck mimic, switches its association from kinesin to KIC, stalling the motor. KIC denies access of the motor to its track by steric interference. Two major features of this regulation, allosteric trapping and steric blocking, are likely to be general for all kinesins.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0811131106