1II6

Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP.

Summary for 1II6

• Entry DOI: 10.2210/pdb1ii6/pdb
• Descriptor: KINESIN-RELATED MOTOR PROTEIN Eg5, NITRATE ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: mg-adp complex, cell cycle
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P52732
• Total number of polymer chains: 2
• Total formula weight: 83138.19

Authors

Turner, J.,Anderson, R.,Guo, J.,Beraud, C.,Sakowicz, R.,Fletterick, R. (deposition date: 2001-04-20, release date: 2001-07-18, Last modification date: 2024-04-03)

Primary citation

Turner, J.,Anderson, R.,Guo, J.,Beraud, C.,Fletterick, R.,Sakowicz, R.
Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker.
J.Biol.Chem., 276:25496-25502, 2001

PubMed Abstract: 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.

PubMed: 11328809
DOI: 10.1074/jbc.M100395200

Experimental method

X-RAY DIFFRACTION (2.1 Å)