Literature summary for 1.1.1.188 extracted from

Moen, S.O.; Fairman, J.W.; Barnes, S.R.; Sullivan, A.; Nakazawa-Hewitt, S.; Van Voorhis, W.C.; Staker, B.L.; Lorimer, D.D.; Myler, P.J.; Edwards, T.E.
Structures of prostaglandin F synthase from the protozoa Leishmania major and Trypanosoma cruzi with NADP (2015), Acta Crystallogr. Sect. F, 71, 609-614.

Search for more literature for 1.1.1.188

Cloned(Commentary)

Cloned (Comment)	Organism
gene P100/11E, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)	Leishmania major
gene Tc00.1047053511287.49, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)	Trypanosoma cruzi

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant apoenzyme or enzyme with bound cofactor NADP+, mixing of 20 mg/ml protein in 25 mM Tris pH 8.0, 200 mM NaCl, 1% v/v glycerol, 1 mM TCEP with reservoir solution. For the apoenzyme, the reservoir solution contains 0.1 M MES-imidazole, pH 6.5, 10% PEG 20 000, 20% PEG 550 MME, 0.02 M glutamic acid, glycine, serine, alanine, and lysine, and for the cofactor complexed enzyme, it contains 0.2 M ammonium acetate, 0.1 M Bis-Tris pH 5.5, 25% PEG 3350, cryoprotectant is 15% ethylene glycol, 16°C, 2-4 weeks, X-ray diffraction structure determination and analysis at 1.25 A and 2.6 A resolution, respectively, molecular replacement	Trypanosoma cruzi
purified recombinant apoenzyme or enzyme with bound cofactor NADPH, mixing of 20 mg/ml protein in 25 mM Tris, pH 8.0, 200 mM NaCl, 1% v/v glycerol, 1 mM TCEP with the reservoir solution containing 0.1 M sodium citrate pH 5.50, 20% PEG 3000 200 mM magnesium chloride, 100 mM Tris, pH 7.0, 10% PEG 8000 for apo- and complexed enzyme, 16°C, 2-4 weeks, X-ray diffraction structure determination and analysis at 1.8 A and 1.6 A resolution, respectively, molecular replacement	Leishmania major

Crystallization (Comment)

Organism

purified recombinant apoenzyme or enzyme with bound cofactor NADP+, mixing of 20 mg/ml protein in 25 mM Tris pH 8.0, 200 mM NaCl, 1% v/v glycerol, 1 mM TCEP with reservoir solution. For the apoenzyme, the reservoir solution contains 0.1 M MES-imidazole, pH 6.5, 10% PEG 20 000, 20% PEG 550 MME, 0.02 M glutamic acid, glycine, serine, alanine, and lysine, and for the cofactor complexed enzyme, it contains 0.2 M ammonium acetate, 0.1 M Bis-Tris pH 5.5, 25% PEG 3350, cryoprotectant is 15% ethylene glycol, 16°C, 2-4 weeks, X-ray diffraction structure determination and analysis at 1.25 A and 2.6 A resolution, respectively, molecular replacement

Trypanosoma cruzi

purified recombinant apoenzyme or enzyme with bound cofactor NADPH, mixing of 20 mg/ml protein in 25 mM Tris, pH 8.0, 200 mM NaCl, 1% v/v glycerol, 1 mM TCEP with the reservoir solution containing 0.1 M sodium citrate pH 5.50, 20% PEG 3000 200 mM magnesium chloride, 100 mM Tris, pH 7.0, 10% PEG 8000 for apo- and complexed enzyme, 16°C, 2-4 weeks, X-ray diffraction structure determination and analysis at 1.8 A and 1.6 A resolution, respectively, molecular replacement

Leishmania major

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+	Leishmania major	-	(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+	-	?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+	Trypanosoma cruzi	-	(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+	-	?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+	Trypanosoma cruzi CL Brener	-	(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Leishmania major	P22045	-	-
Trypanosoma cruzi	Q4DJ07	-	-
Trypanosoma cruzi CL Brener	Q4DJ07	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration followed by a polyether sulfon concentration	Leishmania major
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration followed by a polyether sulfon concentration	Trypanosoma cruzi

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+	-	Leishmania major	(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+	-	?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+	-	Trypanosoma cruzi	(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+	-	?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+	-	Trypanosoma cruzi CL Brener	(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+	-	?

Synonyms

Synonyms	Comment	Organism
LemaA.00019.a.B1	-	Leishmania major
P100/11E	-	Leishmania major
PGF	-	Leishmania major
PGF	-	Trypanosoma cruzi
prostaglandin F synthase	-	Leishmania major
prostaglandin F synthase	-	Trypanosoma cruzi
Tc00.1047053511287.49	-	Trypanosoma cruzi
TrcrA.00019.a.B1	-	Trypanosoma cruzi

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	enzyme PGF is specific for NADP+. Structures of PGF with and without NADP+ and structural differences between the bound and the unbound state of the enzyme with regard to its cofactor	Leishmania major
NADP+	enzyme PGF is specific for NADP+. Structures of PGF with and without NADP+ and structural differences between the bound and the unbound state of the enzyme with regard to its cofactor	Trypanosoma cruzi

General Information

General Information	Comment	Organism
metabolism	enzyme PGF is involved in essential lipid metabolism pathways	Leishmania major
metabolism	enzyme PGF is involved in essential lipid metabolism pathways	Trypanosoma cruzi
additional information	a loop with residues 188-196 in TrcrA.00019.a.B1 shows significant movement between the apoenzyme and holoenzyme. The Trypanosoma cruzi loop becomes ordered and a key interaction with one of the phosphates of NADP at Ser193 is likely to stabilize this region	Trypanosoma cruzi
additional information	a loop with residues 201-205 (disordered) in LemaA.00019.a.B1 shows significant movement between the apoenzyme and holoenzyme. The Leishmania major loop becomes ordered and a key interaction with one of the phosphates of NADP at Gln202 is likely to stabilize this region	Leishmania major