Literature summary for 5.2.1.8 extracted from

Alag, R.; Balakrishna, A.M.; Rajan, S.; Qureshi, I.A.; Shin, J.; Lescar, J.; Grueber, G.; Yoon, H.S.
Structural insights into substrate binding by PvFKBP35, a peptidylprolyl cis-trans isomerase from the human malarial parasite Plasmodium vivax (2013), Eukaryot. Cell, 12, 627-634.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)	Plasmodium vivax

Crystallization (Commentary)

Crystallization (Comment)	Organism
apo-enzyme PvFKBD35 free and in complex with the tetrapeptide substrate succinyl-Ala-Leu-Pro-Phe-p-nitroanilide, sitting-drop vapor diffusion method, mixing of 0.0002 ml of 10 mg/ml protein in 10 mM phosphate, pH 6.8, 137 mM NaCl, and 2.7 mM KCl, with 0.0002 ml of precipitant solution containing 0.1 M Tris-HCl, pH 8.5, 30% w/v PEG 4000, 0.2 M MgCl2, and and equilibration against 0.1 ml precipitant solution, 18°C, X-ray diffraction structure determination and analysis at 1.4 A and 1.65 A resolution, respectively	Plasmodium vivax

Crystallization (Comment)

Organism

apo-enzyme PvFKBD35 free and in complex with the tetrapeptide substrate succinyl-Ala-Leu-Pro-Phe-p-nitroanilide, sitting-drop vapor diffusion method, mixing of 0.0002 ml of 10 mg/ml protein in 10 mM phosphate, pH 6.8, 137 mM NaCl, and 2.7 mM KCl, with 0.0002 ml of precipitant solution containing 0.1 M Tris-HCl, pH 8.5, 30% w/v PEG 4000, 0.2 M MgCl2, and and equilibration against 0.1 ml precipitant solution, 18°C, X-ray diffraction structure determination and analysis at 1.4 A and 1.65 A resolution, respectively

Plasmodium vivax

Protein Variants

Protein Variants	Comment	Organism
Y100A	site-directed mutagenesis, the mutant shows about 10% reduced activity compared to the wild-type enzyme	Plasmodium vivax
Y100E	site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme	Plasmodium vivax
Y100F	site-directed mutagenesis, the mutant shows about 10% reduced activity compared to the wild-type enzyme	Plasmodium vivax
Y100L	site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme	Plasmodium vivax
Y100P	site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme	Plasmodium vivax
Y100R	site-directed mutagenesis, the mutant shows about 40% reduced activity compared to the wild-type enzyme	Plasmodium vivax
Y100W	site-directed mutagenesis, the mutant shows about 30% reduced activity compared to the wild-type enzyme	Plasmodium vivax

Inhibitors

Inhibitors	Comment	Organism	Structure
FK506	an immunosuppressive drug	Plasmodium vivax
Rapamycin	an immunosuppressive drug	Plasmodium vivax

Organism

Organism	UniProt	Comment	Textmining
Plasmodium vivax	A5K8X6	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration to near homogeneity	Plasmodium vivax

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	PPIase proteins catalyze the cis-trans isomerization of the peptidylprolyl bond, molecular interaction between the isomerase and a peptide substrate, overview	Plasmodium vivax	?	-	?
succinyl-Ala-Leu-Pro(omega180)-Phe-4-nitroanilide	the substrate binds to PvFKBD35 in a cis conformation involving residues D55, H67, V73, and I74	Plasmodium vivax	succinyl-Ala-Leu-Pro(omega0)-Phe-4-nitroanilide	-	?

Synonyms

Synonyms	Comment	Organism
FK506 binding protein 35	-	Plasmodium vivax
Peptidylprolyl cis-trans isomerase	-	Plasmodium vivax
PvFKBP35	-	Plasmodium vivax

General Information

General Information	Comment	Organism
additional information	Y100 is a key residue for the catalytic activity, catalytic mechanism of PvFKBP35-mediated cis-trans isomerization of substrate, overview	Plasmodium vivax