1W1N

The solution structure of the FATC Domain of the Protein Kinase TOR1 from yeast

1W1N の概要

• エントリーDOI: 10.2210/pdb1w1n/pdb
• 分子名称: PHOSPHATIDYLINOSITOL 3-KINASE TOR1 (1 entity in total)
• 機能のキーワード: tor, target of rapamycin, ser/thr kinase, redox-regulation, disulfide bond, transferase
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P35169
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3963.47

構造登録者

Dames, S.A.,Mulet, J.M.,Rathgeb-Szabo, K.,Hall, M.N.,Grzesiek, S. (登録日: 2004-06-23, 公開日: 2005-03-16, 最終更新日: 2024-10-23)

主引用文献

Dames, S.A.,Mulet, J.M.,Rathgeb-Szabo, K.,Hall, M.N.,Grzesiek, S.
The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability.
J. Biol. Chem., 280:20558-20564, 2005

PubMed Abstract: The target of rapamycin (TOR) is a highly conserved Ser/Thr kinase that plays a central role in the control of cellular growth. TOR has a characteristic multidomain structure. Only the kinase domain has catalytic function; the other domains are assumed to mediate interactions with TOR substrates and regulators. Except for the rapamycin-binding domain, there are no high-resolution structural data available for TOR. Here, we present a structural, biophysical, and mutagenesis study of the extremely conserved COOH-terminal FATC domain. The importance of this domain for TOR function has been highlighted in several publications. We show that the FATC domain, in its oxidized form, exhibits a novel structural motif consisting of an alpha-helix and a COOH-terminal disulfide-bonded loop between two completely conserved cysteine residues. Upon reduction, the flexibility of the loop region increases dramatically. The structural data, the redox potential of the disulfide bridge, and the biochemical data of a cysteine to serine mutant indicate that the intracellular redox potential can affect the cellular amount of the TOR protein via the FATC domain. Because the amount of TOR mRNA is not changed, the redox state of the FATC disulfide bond is probably influencing the degradation of TOR.

PubMed: 15772072
DOI: 10.1074/jbc.M501116200

実験手法

SOLUTION NMR