1II6

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

1II6 の概要

• エントリーDOI: 10.2210/pdb1ii6/pdb
• 分子名称: KINESIN-RELATED MOTOR PROTEIN Eg5, NITRATE ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: mg-adp complex, cell cycle
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P52732
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83138.19

構造登録者

Turner, J.,Anderson, R.,Guo, J.,Beraud, C.,Sakowicz, R.,Fletterick, R. (登録日: 2001-04-20, 公開日: 2001-07-18, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)