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Literature summary for 2.7.11.31 extracted from

  • Peng, C.; Head-Gordon, T.
    The dynamical mechanism of auto-inhibition of AMP-activated protein kinase (2011), PLoS Comput. Biol., 7, e1002082.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
AMP binding of AMP to the gamma-subunit Schizosaccharomyces pombe

Inhibitors

Inhibitors Comment Organism Structure
additional information dynamical mechanism of autoinhibition of AMP-activated protein kinase, molecular dynamics simulations and modelling, overview. Conformational switch model involving the movement of the kinase domain between an inactive unphosphorylated open state and an active or semi-active phosphorylated closed state, mediated by the autoinhibitory domain (AID). AID inhibits the catalytic function by restraining the kinase domain into an unproductive open conformation, thereby limiting local structural rearrangements, while mutations that disrupt the interactions between the kinase domain and AID allow for both the local structural rearrangement and global interlobe conformational transition. The AID also greatly impacts the structuring and mobility of the activation loop. Binding of AMP to the gamma-subunit changes the interactions between the AID and kinase domain to remove the inhibitory effect of AID to allow the interlobe conformational transition to the closed state. The unphosphorylated KD-AID fragment from Schizosaccharomycespombe (PDB ID 3H4J) is used as a model of the inactive-open state because of its open interlobe conformation, while the phosphorylated kinase domain fragment from Saccharomyces cerevisiae (PDB ID 3DAE) is used as the active-closed state reference, in accord with the experimental structural and mutagenesis analysis. AID inhibits catalytic function by restraining kinase domain to an inactive-open state Schizosaccharomyces pombe

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe
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Synonyms

Synonyms Comment Organism
AMP-activated protein kinase
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 Schizosaccharomyces pombe
Snf1 kinase i.e. sucrose non-fermenting 1 kinase Schizosaccharomyces pombe

General Information

General Information Comment Organism
additional information residues Glu42, Arg81, Asp156, and Phe175 of the isolated kinase domain fragment have greater conformational flexibility in the closed state, with the hinge residue Gly116 exhibiting two conformational basins in the closed state, and Gly115 already in an active-closed state conformation even when the interlobe conformation is open Schizosaccharomyces pombe
physiological function AMP-activated protein kinase (AMPK) maintains the balance between ATP production and energy consumption in eukaryotic cells by responding to the rise of intracellular AMP Schizosaccharomyces pombe