3HYH

Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1

Replaces:  3FAMReplaces:  2EUE

Summary for 3HYH

• Entry DOI: 10.2210/pdb3hyh/pdb
• Descriptor: Carbon catabolite-derepressing protein kinase (2 entities in total)
• Functional Keywords: kinase domain, transferase, atp-binding, carbohydrate metabolism, kinase, membrane, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasm : P06782
• Total number of polymer chains: 2
• Total formula weight: 62694.98

Authors

Rudolph, M.J.,Amodeo, G.A.,Bai, Y.,Tong, L. (deposition date: 2009-06-22, release date: 2009-06-30, Last modification date: 2024-02-21)

Primary citation

Rudolph, M.J.,Amodeo, G.A.,Bai, Y.,Tong, L.
Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1
Biochem.Biophys.Res.Commun., 337:1224-1228, 2005

PubMed Abstract: AMP-activated protein kinase (AMPK) is a master metabolic regulator, and is an important target for drug development against diabetes, obesity, and other diseases. AMPK is a hetero-trimeric enzyme, with a catalytic (alpha) subunit, and two regulatory (beta and gamma) subunits. Here we report the crystal structure at 2.2A resolution of the protein kinase domain (KD) of the catalytic subunit of yeast AMPK (commonly known as SNF1). The Snf1-KD structure shares strong similarity to other protein kinases, with a small N-terminal lobe and a large C-terminal lobe. Two negative surface patches in the structure may be important for the recognition of the substrates of this kinase.

PubMed: 16236260
DOI: 10.1016/j.bbrc.2005.09.181

Experimental method

X-RAY DIFFRACTION (2.2 Å)