Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain

Masato Akutsu, Masato Kawasaki, Yohei Katoh, Tomoo Shiba, Yoshiki Yamaguchi, Ryuichi Kato, Koichi Kato, Kazuhisa Nakayama, Soichi Wakatsuki

研究成果: Article査読

28 被引用数 (Scopus)

抄録

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 α1 and α2. NMR and biochemical data revealed that the N-terminal half of helix α3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1.

本文言語English
ページ(範囲)5385-5391
ページ数7
ジャーナルFEBS Letters
579
24
DOI
出版ステータスPublished - 2005 10月 10
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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