Structural highlights
3mn3 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Related: | 3hyh, 2qlv, 2nyc, 2nye |
Gene: | SNF1, CAT1, CCR1, GLC2, PAS14, YDR477W, D8035.20 (Saccharomyces cerevisiae) |
Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 |
Resources: | FirstGlance, OCA, RCSB, PDBsum |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1.,Rudolph MJ, Amodeo GA, Tong L Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):999-1002. Epub 2010 Aug 21. PMID:20823513[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rudolph MJ, Amodeo GA, Tong L. An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):999-1002. Epub 2010 Aug 21. PMID:20823513 doi:10.1107/S1744309110028265