Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase

Robert Townley, Lawrence Shapiro

Research output: Contribution to journalArticle

144 Citations (Scopus)

Abstract

The 5′-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Here, we report crystal structures at 2.9 and 2.6 Å resolution for ATP- and AMP-bound forms of a core αβγ adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the γ subunit, with their respective phosphate groups positioned near function-impairing mutants. Unexpectedly, ATP binds without counterions, amplifying its electrostatic effects on a critical regulatory region where all three subunits converge.

Original languageEnglish (US)
Pages (from-to)1726-1729
Number of pages4
JournalScience
Volume315
Issue number5819
DOIs
StatePublished - Mar 23 2007
Externally publishedYes

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AMP-Activated Protein Kinases
Schizosaccharomyces
Adenosine Monophosphate
Adenosine Triphosphate
Protein Kinases
Nucleic Acid Regulatory Sequences
Static Electricity
Phosphates

ASJC Scopus subject areas

  • General

Cite this

Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase. / Townley, Robert; Shapiro, Lawrence.

In: Science, Vol. 315, No. 5819, 23.03.2007, p. 1726-1729.

Research output: Contribution to journalArticle

Townley, Robert ; Shapiro, Lawrence. / Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase. In: Science. 2007 ; Vol. 315, No. 5819. pp. 1726-1729.
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