1TXQ

Crystal structure of the EB1 C-terminal domain complexed with the CAP-Gly domain of p150Glued

1TXQ の概要

• エントリーDOI: 10.2210/pdb1txq/pdb
• 分子名称: Dynactin 1, Microtubule-associated protein RP/EB family member 1 (3 entities in total)
• 機能のキーワード: protein complex, structural protein-protein binding complex, structural protein/protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: Q14203; Cytoplasm, cytoskeleton: Q15691
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19706.67

構造登録者

Hayashi, I.,Ikura, M. (登録日: 2004-07-06, 公開日: 2005-09-13, 最終更新日: 2024-03-13)

主引用文献

Hayashi, I.,Wilde, A.,Mal, T.K.,Ikura, M.
Structural Basis for the Activation of Microtubule Assembly by the EB1 and p150(Glued) Complex
Mol.Cell, 19:449-460, 2005

PubMed Abstract: Plus-end tracking proteins, such as EB1 and the dynein/dynactin complex, regulate microtubule dynamics. These proteins are thought to stabilize microtubules by forming a plus-end complex at microtubule growing ends with ill-defined mechanisms. Here we report the crystal structure of two plus-end complex components, the carboxy-terminal dimerization domain of EB1 and the microtubule binding (CAP-Gly) domain of the dynactin subunit p150Glued. Each molecule of the EB1 dimer contains two helices forming a conserved four-helix bundle, while also providing p150Glued binding sites in its flexible tail region. Combining crystallography, NMR, and mutational analyses, our studies reveal the critical interacting elements of both EB1 and p150Glued, whose mutation alters microtubule polymerization activity. Moreover, removal of the key flexible tail from EB1 activates microtubule assembly by EB1 alone, suggesting that the flexible tail negatively regulates EB1 activity. We, therefore, propose that EB1 possesses an auto-inhibited conformation, which is relieved by p150Glued as an allosteric activator.

PubMed: 16109370
DOI: 10.1016/j.molcel.2005.06.034

実験手法

X-RAY DIFFRACTION (1.8 Å)