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Crystal Structure of the Protein Kinase Domain of Yeast AMP-Activated Protein Kinase Snf1

Journal Article · · Biochem. Biophys. Res. Commun.

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 2.2 Angstrom 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.

Research Organization:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Organization:
Doe - Office Of Science
DOE Contract Number:
AC02-98CH10886
OSTI ID:
913706
Report Number(s):
BNL--78274-2007-JA
Journal Information:
Biochem. Biophys. Res. Commun., Journal Name: Biochem. Biophys. Res. Commun. Vol. 337; ISSN BBRCA9; ISSN 0006-291X
Country of Publication:
United States
Language:
English

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