4EAG

Co-crystal structure of an chimeric AMPK core with ATP

4EAG の概要

• エントリーDOI: 10.2210/pdb4eag/pdb
• 関連するPDBエントリー: 4EAI 4EAJ 4EAK 4EAL
• 分子名称: EG:132E8.2 protein, 5'-AMP-activated protein kinase subunit beta-1, 5'-AMP-activated protein kinase subunit gamma-1, ... (6 entities in total)
• 機能のキーワード: ampk, transferase
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 63303.58

構造登録者

Chen, L.,Wang, J.,Zhang, Y.-Y.,Yan, S.F.,Neumann, D.,Schlattner, U.,Wang, Z.-X.,Wu, J.-W. (登録日: 2012-03-22, 公開日: 2012-06-06, 最終更新日: 2023-11-08)

主引用文献

Chen, L.,Wang, J.,Zhang, Y.-Y.,Yan, S.F.,Neumann, D.,Schlattner, U.,Wang, Z.-X.,Wu, J.-W.
AMP-activated protein kinase undergoes nucleotide-dependent conformational changes
Nat.Struct.Mol.Biol., 19:716-718, 2012

PubMed Abstract: The energy sensor AMP-activated protein kinase (AMPK) is a heterotrimeric complex that is allosterically activated by AMP binding to the γ subunit. Cocrystal structures of the mammalian AMPK core reveal occlusion of nucleotide-binding site 3 of the γ subunit in the presence of ATP. However, site 3 is occupied in the presence of AMP. Mutagenesis studies indicate that sites 3 and 4 are important for AMPK allosteric activation.

PubMed: 22659875
DOI: 10.1038/nsmb.2319

実験手法

X-RAY DIFFRACTION (2.701 Å)