Structural highlights
Function[SNF1_YEAST] Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAMP-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. Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1.,Rudolph MJ, Amodeo GA, Bai Y, Tong L Biochem Biophys Res Commun. 2005 Dec 2;337(4):1224-8. Epub 2005 Oct 7. PMID:16236260[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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