1ii6
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Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP.
OverviewOverview
Success of mitosis depends upon the coordinated and regulated activity of, many cellular factors, including kinesin motor proteins, which are, required for the assembly and function of the mitotic spindle. Eg5 is a, kinesin implicated in the formation of the bipolar spindle and its, movement prior to and during anaphase. We have determined the crystal, structure of the Eg5 motor domain with ADP-Mg bound. This structure, revealed a new intramolecular binding site of the neck-linker. In other, kinesins, the neck-linker has been shown to be a critical mechanical, element for force generation. The neck-linker of conventional kinesin is, believed to undergo an ordered-to-disordered transition as it translocates, along a microtubule. The structure of Eg5 showed an ordered neck-linker, conformation in a position never observed previously. The docking of the, neck-linker relies upon residues conserved only in the Eg5 subfamily of, kinesin motors. Based on this new information, we suggest that the, neck-linker of Eg5 may undergo an ordered-to-ordered transition during, force production. This ratchet-like mechanism is consistent with the, biological activity of Eg5.
About this StructureAbout this Structure
1II6 is a Single protein structure of sequence from Homo sapiens with NO3, MG and ADP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker., Turner J, Anderson R, Guo J, Beraud C, Fletterick R, Sakowicz R, J Biol Chem. 2001 Jul 6;276(27):25496-502. Epub 2001 Apr 27. PMID:11328809
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