Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain
Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain
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DOI：
10.1016/j.febslet.2005.08.076
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发表时间：
2005-10-10
期刊：
影响因子：
3.5
通讯作者：
Wakatsuki, S
中科院分区：
文献类型：
--
作者：
Akutsu, M;Kawasaki, M;Wakatsuki, S
Tom1 （Myb1的靶标）被认为通过其GAT （GGA和Tom1）结构域与泛素的相互作用参与泛素化蛋白的运输。在这里，我们证明了Tom1-GAT的三螺旋束有两个泛素结合位点，可以识别泛素的疏水性Ile44表面。复杂的晶体结构表明，第一个位点是螺旋α 1和α 2上的疏水斑块。核磁共振和生化数据显示，Tom1-GAT的螺旋α 3的n端半构成了第二个更强的结合位点。双面泛素结合增强了Tom1对泛素化蛋白的识别效率。(c) 2005年欧洲生化学会联合会。Elsevier B.V.版权所有。
Tom1 (Target of Myb1) is suggested to be involved in the transport of ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of ubiquitin. The complex crystal structure demonstrates that the first site is a hydrophobic patch on helices alpha 1 and alpha 2. NMR and biochemical data revealed that the N-terminal half of helix alpha 3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.