2OOX: Crystal Structure Of The Adenylate Sensor From Amp-activated Protein Kinase Complexed With Amp

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 A resolution for ATP- and AMP-bound forms of a core alphabetagamma adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the gamma 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.
PDB ID: 2OOXDownload
MMDB ID: 44262
PDB Deposition Date: 2007/1/26
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Similar Structures:
Biological Unit for 2OOX: hexameric; determined by author
Molecular Components in 2OOX
Label Count Molecule
Proteins (6 molecules)
Snf1-like Protein Kinase Ssp2(Gene symbol: ssp2)
Molecule annotation
Spcc1919.03c Protein(Gene symbol: amk2)
Molecule annotation
Hypothetical Protein C1556.08c in Chromosome I(Gene symbol: cbs2)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB