2FH9

Structure and dimerization of the kinase domain from yeast Snf1

2FH9 の概要

• エントリーDOI: 10.2210/pdb2fh9/pdb
• 分子名称: Snf1 kinase (2 entities in total)
• 機能のキーワード: kinase domain; dimer, signaling protein, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm : P06782
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31255.40

構造登録者

Nayak, V. (登録日: 2005-12-23, 公開日: 2006-03-28, 最終更新日: 2024-02-14)

主引用文献

Nayak, V.,Zhao, K.,Wyce, A.,Schwartz, M.F.,Lo, W.S.,Berger, S.L.,Marmorstein, R.
Structure and Dimerization of the Kinase Domain from Yeast Snf1, a Member of the Snf1/AMPK Protein Family
Structure, 14:477-485, 2006

PubMed Abstract: The Snf1/AMPK kinases are intracellular energy sensors, and the AMPK pathway has been implicated in a variety of metabolic human disorders. Here we report the crystal structure of the kinase domain from yeast Snf1, revealing a bilobe kinase fold with greatest homology to cyclin-dependant kinase-2. Unexpectedly, the crystal structure also reveals a novel homodimer that we show also forms in solution, as demonstrated by equilibrium sedimentation, and in yeast cells, as shown by coimmunoprecipitation of differentially tagged intact Snf1. A mapping of sequence conservation suggests that dimer formation is a conserved feature of the Snf1/AMPK kinases. The conformation of the conserved alphaC helix, and the burial of the activation segment and substrate binding site within the dimer, suggests that it represents an inactive form of the kinase. Taken together, these studies suggest another layer of kinase regulation within the Snf1/AMPK family, and an avenue for development of AMPK-specific activating compounds.

PubMed: 16531232
DOI: 10.1016/j.str.2005.12.008

実験手法

X-RAY DIFFRACTION (2.8 Å)