Literature summary for 2.7.11.11 extracted from

Akamine, P.; Madhusudan; Wu, J.; Xuong, N.H.; Ten Eyck, L.F.; Taylor, S.S.
Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure (2003), J. Mol. Biol., 327, 159-171.

Search for more literature for 2.7.11.11

Activating Compound

Activating Compound	Comment	Organism	Structure
cAMP	dependent on	Mus musculus

Cloned(Commentary)

Cloned (Comment)	Organism
expression of catalytic subunit PKA Calpha in Escherichia coli strain BL21	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant catalytic apo-subunit apo-PKA Calpha phosphorylated at Ser10, Thr197, and Ser338, hanging drop vapour diffusion method, 4°C, 0.02 ml of 7.5 mg/ml protein in solution 0.1 mM bicine buffer, pH 8.0, 150 mM ammonium acetate, 10 mM 2-mercaptoethanol, and 3% 2-methyl-2,4-pentanediol versus 1 ml reservoir solution containing 0.1 mM Tris-HCl, pH 7.5, and 10-20% v/v 2-methyl-2,4-pentanediol, temperature-sensitive crystals need 6 months to 1 year to grow, cryoprotection by a gradient of 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement	Mus musculus

Crystallization (Comment)

Organism

purified recombinant catalytic apo-subunit apo-PKA Calpha phosphorylated at Ser10, Thr197, and Ser338, hanging drop vapour diffusion method, 4°C, 0.02 ml of 7.5 mg/ml protein in solution 0.1 mM bicine buffer, pH 8.0, 150 mM ammonium acetate, 10 mM 2-mercaptoethanol, and 3% 2-methyl-2,4-pentanediol versus 1 ml reservoir solution containing 0.1 mM Tris-HCl, pH 7.5, and 10-20% v/v 2-methyl-2,4-pentanediol, temperature-sensitive crystals need 6 months to 1 year to grow, cryoprotection by a gradient of 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement

Mus musculus

Inhibitors

Inhibitors	Comment	Organism	Structure
IP20	iodinated inhibitor peptide substrate	Mus musculus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	as MgATP2-, binding site structure	Mus musculus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
40800	-	x * 40800, recombinant catalytic subunit PKA Calpha, SDS-PAGE	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	the enzyme autophosphorylates at Ser10, Thr197, and Ser338 of catalytic subunit PKA Calpha	Mus musculus

Purification (Commentary)

Purification (Comment)	Organism
recombinant catalytic subunit PKA Calpha from Escherichia coli strain BL21 by P11 cellulose and ion exchange chromatography	Mus musculus

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate	active site residues and structure, mechanism of ligand binding and ligand-induced conformational changes	Mus musculus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + SP20	substrate peptide, the C subunit SP20-binding residues are E203, F129, E170, E230, D166, and K168	Mus musculus	ADP + SP20 phosphate	-	?
additional information	the enzyme autophosphorylates at Ser10, Thr197, and Ser338 of PKA Calpha, substrate-induced conformational changes	Mus musculus	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 40800, recombinant catalytic subunit PKA Calpha, SDS-PAGE	Mus musculus
More	apoenzyme structure analysis, hydrophobic core network, overview	Mus musculus

Synonyms

Synonyms	Comment	Organism
PKA Calpha	-	Mus musculus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	as MgATP2-, binding site structure	Mus musculus