1SDM

Crystal structure of kinesin-like calmodulin binding protein

1SDM の概要

• エントリーDOI: 10.2210/pdb1sdm/pdb
• 分子名称: kinesin heavy chain-like protein, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: kinesin, minus-end directed, ca2+/calmodulin regulated, transport protein
• 由来する生物種: Solanum tuberosum (potato)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41880.42

構造登録者

Vinogradova, M.V.,Reddy, V.S.,Reddy, A.S.,Sablin, E.P.,Fletterick, R.J. (登録日: 2004-02-13, 公開日: 2004-06-22, 最終更新日: 2023-08-23)

主引用文献

Vinogradova, M.V.,Reddy, V.S.,Reddy, A.S.,Sablin, E.P.,Fletterick, R.J.
Crystal structure of kinesin regulated by Ca(2+)-calmodulin.
J.Biol.Chem., 279:23504-23509, 2004

PubMed Abstract: Kinesins orchestrate cell division by controlling placement of chromosomes. Kinesins must be precisely regulated or else cell division fails. Calcium, a universal second messenger in eukaryotes, and calmodulin regulate some kinesins by causing the motor to dissociate from its biological track, the microtubule. Our focus was the mechanism of calcium regulation of kinesin at atomic resolution. Here we report the crystal structure of kinesin-like calmodulin-binding protein (KCBP) from potato, which was resolved to 2.3 A. The structure reveals three subdomains of the regulatory machinery located at the C terminus extension of the kinesin motor. Calmodulin that is activated by Ca2+ ions binds to an alpha-helix positioned on the microtubule-binding face of kinesin. A negatively charged segment following this helix competes with microtubules. A mimic of the conventional kinesin neck, connecting the calmodulin-binding helix to the KCBP motor core, links the regulatory machine to the kinesin catalytic cycle. Together with biochemical data, the crystal structure suggests that Ca(2+)-calmodulin inhibits the binding of KCBP to microtubules by blocking the microtubule-binding sites on KCBP.

PubMed: 14988396
DOI: 10.1074/jbc.M400741200

実験手法

X-RAY DIFFRACTION (2.3 Å)