3H4S

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

Summary for 3H4S

• Entry DOI: 10.2210/pdb3h4s/pdb
• Descriptor: Kinesin-like calmodulin-binding protein, KCBP interacting Ca2+-binding protein, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: kinesin, motor protein, regulation, complex, calcium, ef-hand, calmodulin, atp-binding, microtubule, nucleotide-binding, motor protein-calcium binding protein complex, motor protein/calcium binding protein
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress); More
• Total number of polymer chains: 2
• Total formula weight: 59739.12

Authors

Vinogradova, M.V. (deposition date: 2009-04-20, release date: 2009-05-19, Last modification date: 2023-09-06)

Primary citation

Vinogradova, M.V.,Malanina, G.G.,Reddy, A.S.,Fletterick, R.J.
Structure of the complex of a mitotic kinesin with its calcium binding regulator.
Proc.Natl.Acad.Sci.USA, 106:8175-8179, 2009

PubMed Abstract: 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 Ca(2+) 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.

PubMed: 19416847
DOI: 10.1073/pnas.0811131106

Experimental method

X-RAY DIFFRACTION (2.4 Å)