Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1.
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.
Rudolph
Michael J
MJ
Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
Amodeo
Gabriele A
GA
Bai
Yun
Y
Tong
Liang
L
D000249:Adenosine Monophosphate / Q000494:pharmacology*; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D019281:Dimerization; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000187:drug effects* / Q000201:enzymology* / Q000235:genetics; D040681:Structural Homology, Protein
D000249:Adenosine Monophosphate; C071570:SNF1-related protein kinases; D017346:Protein Serine-Threonine Kinases