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Literature summary for 2.7.11.11 extracted from

  • Vigil, D.; Lin, J.H.; Sotriffer, C.A.; Pennypacker, J.K.; McCammon, J.A.; Taylor, S.S.
    A simple electrostatic switch important in the activation of type I protein kinase A by cyclic AMP (2006), Protein Sci., 15, 113-121.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
cAMP dynamics of the binding domain structure, molecular binding mechanism, overview Bos taurus

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant subunit RIalpha residues 91-244 constructs, containing the minimal motifs for cAMP-dependent tight binding of subunit C, in Escherichia coli strain BL21(DE3) Bos taurus

Protein Variants

Protein Variants Comment Organism
I204A site-directed mutagenesis, subunit RIalpha residue mutation, slightly impaired activation of subunit C, mutant show a slightly lower melting temperature compared to the wild-type subunit RIalpha Bos taurus
L203A site-directed mutagenesis, subunit RIalpha residue mutation, slightly impaired activation of subunit C, mutant show a slightly lower melting temperature compared to the wild-type subunit RIalpha Bos taurus
R241A site-directed mutagenesis, subunit RIalpha residue mutation, slightly impaired activation of subunit C, mutant show a slightly lower melting temperature compared to the wild-type subunit RIalpha Bos taurus
Y229A site-directed mutagenesis, subunit RIalpha residue mutation, slightly impaired activation of subunit C, mutant show a slightly lower melting temperature compared to the wild-type subunit RIalpha Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant subunit RIalpha residues 91-244 construct dimers from Escherichia coli strain BL21(DE3) by cAMP affinity chromatography, dialysis, and gel filtration Bos taurus

Reaction

Reaction Comment Organism Reaction ID
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate activation mechanism Bos taurus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + Kemptide LRRASLG peptide substrate, activity of the catalytic subunit C Bos taurus ADP + Kemptide phosphate
-
 ?
additional information cAMP binds to the helical subunit C binding regions relayed by the highly dynamic switch of the C-helix of subunit RIalpha, which is linked to cAMP by a salt bridge essential for activation Bos taurus ?
-
 ?

Subunits

Subunits Comment Organism
More determination of cAMP binding and interaction structures of subunits C and RIalpha, overview Bos taurus

Synonyms

Synonyms Comment Organism
type I PKA
-
 Bos taurus
type I protein kinase A
-
 Bos taurus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bos taurus