4EAG

Co-crystal structure of an chimeric AMPK core with ATP

Summary for 4EAG

• Entry DOI: 10.2210/pdb4eag/pdb
• Related: 4EAI 4EAJ 4EAK 4EAL
• Descriptor: EG:132E8.2 protein, 5'-AMP-activated protein kinase subunit beta-1, 5'-AMP-activated protein kinase subunit gamma-1, ... (6 entities in total)
• Functional Keywords: ampk, transferase
• Biological source: Drosophila melanogaster (Fruit fly); More
• Total number of polymer chains: 3
• Total formula weight: 63303.58

Authors

Chen, L.,Wang, J.,Zhang, Y.-Y.,Yan, S.F.,Neumann, D.,Schlattner, U.,Wang, Z.-X.,Wu, J.-W. (deposition date: 2012-03-22, release date: 2012-06-06, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.701 Å)