1mkj
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Human Kinesin Motor Domain With Docked Neck Linker
OverviewOverview
Crystal structures of the molecular motor kinesin show conformational, variability in a structural element called the neck linker. Conformational, change in the neck linker, initiated by ATP exchange, is thought to drive, the movement of kinesin along the microtubule track. We use site-specific, EPR measurements to show that when microtubules are absent, the neck, linker exists in equilibrium between two structural states (disordered and, 'docked'). The active site nucleotide does not control the position taken, by the neck linker. However, we find that sulfate can specifically bind, near the nucleotide site and stabilize the docked neck linker, conformation, which we confirmed by solving a new crystal structure., Comparing the crystal structures of our construct with the docked or, undocked neck linker reveals how microtubule binding may activate the, nucleotide-sensing mechanism of kinesin, allowing neck linker transitions, to power motility.
About this StructureAbout this Structure
1MKJ is a Single protein structure of sequence from Homo sapiens with MG, SO4 and ADP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy., Sindelar CV, Budny MJ, Rice S, Naber N, Fletterick R, Cooke R, Nat Struct Biol. 2002 Nov;9(11):844-8. PMID:12368902
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