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

Robert Townley, Lawrence Shapiro

Research output: Contribution to journalArticlepeer-review

148 Scopus citations

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

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase'. Together they form a unique fingerprint.

Cite this