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Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1

Author

Listed:
  • Gabriele A. Amodeo

    (Columbia University, New York, New York 10027, USA)

  • Michael J. Rudolph

    (Columbia University, New York, New York 10027, USA)

  • Liang Tong

    (Columbia University, New York, New York 10027, USA)

Abstract

AMP-activated protein kinase is a central regulator of energy homeostasis in mammals, and the Saccharomyces cerevisiae homologue SNF1 is essential for responses to nutrient starvation. This structure reveals features such as the ligand-binding site in the γ-subunit, the carbohydrate-binding domain in the β-subunit and a regulatory sequence in the α-subunit.

Suggested Citation

  • Gabriele A. Amodeo & Michael J. Rudolph & Liang Tong, 2007. "Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1," Nature, Nature, vol. 449(7161), pages 492-495, September.
    • Handle: RePEc:nat:nature:v:449:y:2007:i:7161:d:10.1038_nature06127
    DOI: 10.1038/nature06127
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