3MN3

An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1

3MN3 の概要

• エントリーDOI: 10.2210/pdb3mn3/pdb
• 関連するPDBエントリー: 2NYC 2NYE 2QLV 3HYH
• 分子名称: Carbon catabolite-derepressing protein kinase (2 entities in total)
• 機能のキーワード: snf1, kinase domain, autoinhibitory region, transferase
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• 細胞内の位置: Nucleus membrane; Peripheral membrane protein: P06782
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31028.22

構造登録者

Rudolph, M.J.,Amodeo, G.A.,Tong, L. (登録日: 2010-04-20, 公開日: 2010-09-15, 最終更新日: 2024-02-21)

主引用文献

Rudolph, M.J.,Amodeo, G.A.,Tong, L.
An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1.
Acta Crystallogr.,Sect.F, 66:999-1002, 2010

PubMed Abstract: AMP-activated protein kinase (AMPK) is a master metabolic regulator for controlling cellular energy homeostasis. Its homolog in yeast, SNF1, is activated in response to glucose depletion and other stresses. The catalytic (alpha) subunit of AMPK/SNF1 in yeast (Snf1) contains a protein Ser/Thr kinase domain (KD), an auto-inhibitory domain (AID) and a region that mediates interactions with the two regulatory (beta and gamma) subunits. Here, the crystal structure of residues 41-440 of Snf1, which include the KD and AID, is reported at 2.4 A resolution. The AID is completely disordered in the crystal. A new inhibited conformation of the KD is observed in a DFG-out conformation and with the glycine-rich loop adopting a structure that blocks ATP binding to the active site.

PubMed: 20823513
DOI: 10.1107/S1744309110028265

実験手法

X-RAY DIFFRACTION (2.38 Å)