1WRD
Crystal structure of Tom1 GAT domain in complex with ubiquitin
1WRD の概要
エントリーDOI | 10.2210/pdb1wrd/pdb |
分子名称 | Target of Myb protein 1, Ubiquitin (3 entities in total) |
機能のキーワード | three-helix bundle, ubiquitin-binding protein, protein transport-signaling protein complex, protein transport/signaling protein |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Cytoplasm (Probable): O60784 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 20379.28 |
構造登録者 | Akutsu, M.,Kawasaki, M.,Katoh, Y.,Shiba, T.,Yamaguchi, Y.,Kato, R.,Kato, K.,Nakayama, K.,Wakatsuki, S. (登録日: 2004-10-14, 公開日: 2005-10-11, 最終更新日: 2024-03-13) |
主引用文献 | Akutsu, M.,Kawasaki, M.,Katoh, Y.,Shiba, T.,Yamaguchi, Y.,Kato, R.,Kato, K.,Nakayama, K.,Wakatsuki, S. Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain. Febs Lett., 579:5385-5391, 2005 Cited by PubMed Abstract: 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 alpha1 and alpha2. NMR and biochemical data revealed that the N-terminal half of helix alpha3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1. PubMed: 16199040DOI: 10.1016/j.febslet.2005.08.076 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.75 Å) |
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