3MN3

An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1

Summary for 3MN3

• Entry DOI: 10.2210/pdb3mn3/pdb
• Related: 2NYC 2NYE 2QLV 3HYH
• Descriptor: Carbon catabolite-derepressing protein kinase (2 entities in total)
• Functional Keywords: snf1, kinase domain, autoinhibitory region, transferase
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• Cellular location: Nucleus membrane; Peripheral membrane protein: P06782
• Total number of polymer chains: 1
• Total formula weight: 31028.22

Authors

Rudolph, M.J.,Amodeo, G.A.,Tong, L. (deposition date: 2010-04-20, release date: 2010-09-15, Last modification date: 2024-02-21)

Primary citation

Rudolph, M.J.,Amodeo, G.A.,Tong, L.
An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1.
Acta Crystallogr.,Sect.F, 66:999-1002, 2010

PubMed Abstract: AMP-activated protein kinase (AMPK) is a master metabolic regulator for controlling cellular energy homeostasis. Its homolog in yeast, SNF1, is activated in response to glucose depletion and other stresses. The catalytic (alpha) subunit of AMPK/SNF1 in yeast (Snf1) contains a protein Ser/Thr kinase domain (KD), an auto-inhibitory domain (AID) and a region that mediates interactions with the two regulatory (beta and gamma) subunits. Here, the crystal structure of residues 41-440 of Snf1, which include the KD and AID, is reported at 2.4 A resolution. The AID is completely disordered in the crystal. A new inhibited conformation of the KD is observed in a DFG-out conformation and with the glycine-rich loop adopting a structure that blocks ATP binding to the active site.

PubMed: 20823513
DOI: 10.1107/S1744309110028265

Experimental method

X-RAY DIFFRACTION (2.38 Å)