Literature summary for 2.7.11.11 extracted from

Littler, D.R.; Bullen, H.E.; Harvey, K.L.; Beddoe, T.; Crabb, B.S.; Rossjohn, J.; Gilson, P.R.
Disrupting the allosteric interaction between the Plasmodium falciparum cAMP-dependent kinase and its regulatory subunit (2016), J. Biol. Chem., 291, 25375-25386 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
cAMP	the regulatory subunit of Plasmodium falciparum protein kinase A (PfPKA-R) holds the kinase's catalytic subunit (C) in an inactive state by exerting an allosteric inhibitory effect. When two cAMP molecules bind to PKA-R, they stabilize a structural conformation that facilitates its dissociation, freeing PKA-C to phosphorylate downstream substrates such as apical membrane antigen 1	Plasmodium falciparum

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Plasmodium falciparum

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method at 4°C	Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + apical membrane antigen 1	Plasmodium falciparum	-	ADP + phosphorylated apical membrane antigen 1	-	?

Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum	Q7KQK0	cAMP-dependent protein kinase regulatory subunit	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + apical membrane antigen 1	-	Plasmodium falciparum	ADP + phosphorylated apical membrane antigen 1	-	?

Synonyms

Synonyms	Comment	Organism
PKA	-	Plasmodium falciparum
protein kinase A	-	Plasmodium falciparum

General Information

General Information	Comment	Organism
evolution	cAMP-dependent protein kinases are a major regulator of signal transduction that arose prior to the origin of multicellularity in eukaryotes. In mammalian protein kinase A (PKAs), the two binding sites of the regulatpory R subunits display positive cooperativity upon cAMP binding. The C-terminal CBD2, or B site, is always exposed and immediately available for nucleotide binding. When this site is occupied, it stabilizes structural changes within CBD1 that drastically increase its affinity for cAMP and promote subunit dissociation and hence activation. The regulatory subunit of Plasmodium falciparum protein kinase A (PfPKA-R) utilizes a similar two-state cooperative binding mechanism that provides an enthalpically driven interaction with nanomolar affinity for cAMP, as in vertebrates	Plasmodium falciparum
malfunction	uncontrolled premature activation of cAMP-dependent protein kinase regulatory subunit (PfPKA-R) is disruptive to parasite survival	Plasmodium falciparum
physiological function	cAMP-dependent protein kinases are a major regulator of signal transduction	Plasmodium falciparum

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Release 2023.1 (January 2023)