2NYC

Crystal structure of the Bateman2 domain of yeast Snf4

2NYC の概要

• エントリーDOI: 10.2210/pdb2nyc/pdb
• 関連するPDBエントリー: 2NYE
• 分子名称: Nuclear protein SNF4 (2 entities in total)
• 機能のキーワード: bateman2 domain, snf4, amp kinase, protein binding
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus : P12904
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16174.68

構造登録者

Rudolph, M.J.,Amodeo, G.A.,Iram, S.,Hong, S.,Pirino, G.,Carlson, M.,Tong, L. (登録日: 2006-11-20, 公開日: 2006-12-12, 最終更新日: 2023-12-27)

主引用文献

Rudolph, M.J.,Amodeo, G.A.,Iram, S.,Hong, S.P.,Pirino, G.,Carlson, M.,Tong, L.
Structure of the Bateman2 domain of yeast Snf4: dimeric association and relevance for AMP binding.
Structure, 15:65-74, 2007

PubMed Abstract: AMP-activated protein kinase (AMPK) is a central regulator of energy homeostasis in mammals. AMP is believed to control the activity of AMPK by binding to the gamma subunit of this heterotrimeric enzyme. This subunit contains two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. No structural information is currently available on this subunit, and the molecular basis for its interactions with AMP is not well understood. We report here the crystal structure at 1.9 Angstrom resolution of the Bateman2 domain of Snf4, the gamma subunit of the yeast ortholog of AMPK. The structure revealed a dimer of the Bateman2 domain, and this dimerization is supported by our light-scattering, mutagenesis, and biochemical studies. There is a prominent pocket at the center of this dimer, and most of the disease-causing mutations are located in or near this pocket.

PubMed: 17223533
DOI: 10.1016/j.str.2006.11.014

実験手法

X-RAY DIFFRACTION (1.9 Å)