2QRD

Crystal Structure of the Adenylate Sensor from AMP-activated Protein Kinase in complex with ADP and ATP

Summary for 2QRD

• Entry DOI: 10.2210/pdb2qrd/pdb
• Related: 2QR1 2QRC 2QRE
• Descriptor: SNF1-like protein kinase ssp2, SPCC1919.03c protein, Protein C1556.08c, ... (6 entities in total)
• Functional Keywords: ampk, adp, atp-binding, kinase, nucleotide-binding, serine/threonine-protein kinase, transferase, cbs domain
• Biological source: Schizosaccharomyces pombe (fission yeast); More
• Cellular location: Cytoplasm: P78789
• Total number of polymer chains: 6
• Total formula weight: 131292.78

Authors

Jin, X.,Townley, R.,Shapiro, L. (deposition date: 2007-07-28, release date: 2007-10-23, Last modification date: 2023-08-30)

Primary citation

Jin, X.,Townley, R.,Shapiro, L.
Structural Insight into AMPK Regulation: ADP Comes into Play.
Structure, 15:1285-1295, 2007

PubMed Abstract: The AMP-activated protein kinase (AMPK), a sensor of cellular energy status found in all eukaryotes, responds to changes in intracellular adenosine nucleotide levels resulting from metabolic stresses. Here we describe crystal structures of a heterotrimeric regulatory core fragment from Schizosaccharomyces pombe AMPK in complex with ADP, ADP/AMP, ADP/ATP, and 5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranotide (AICAR phosphate, or ZMP), a well-characterized AMPK activator. Prior crystallographic studies had revealed a single site in the gamma subunit that binds either ATP or AMP within Bateman domain B. Here we show that ZMP binds at this site, mimicking the binding of AMP. An analogous site in Bateman domain A selectively accommodates ADP, which binds in a distinct manner that also involves direct ligation to elements from the beta subunit. These observations suggest a possible role for ADP in regulating AMPK response to changes in cellular energy status.

PubMed: 17937917
DOI: 10.1016/j.str.2007.07.017

Experimental method

X-RAY DIFFRACTION (2.41 Å)