4eag | pdb_00004eag

Co-crystal structure of an chimeric AMPK core with ATP

spinqualitylabelsall models 4eag, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4eag is a 3 chain structure with sequence from Drosophila melanogaster and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.701Å Ligands: ATP, TAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O18645_DROME Publication Abstract from PubMed The energy sensor AMP-activated protein kinase (AMPK) is a heterotrimeric complex that is allosterically activated by AMP binding to the gamma subunit. Cocrystal structures of the mammalian AMPK core reveal occlusion of nucleotide-binding site 3 of the gamma 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. AMP-activated protein kinase undergoes nucleotide-dependent conformational changes.,Chen L, Wang J, Zhang YY, Yan SF, Neumann D, Schlattner U, Wang ZX, Wu JW Nat Struct Mol Biol. 2012 Jun 3;19(7):716-8. doi: 10.1038/nsmb.2319. PMID:22659875 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also AMP-activated protein kinase 3D structures

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