Literature summary for 1.14.11.2 extracted from

Schnicker, N.; Dey, M.
Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracis (2016), Acta Crystallogr. Sect. D, 72, 675-681 .

Search for more literature for 1.14.11.2

Cloned(Commentary)

Cloned (Comment)	Organism
gene GBAA_4459, recombinant enzyme expression in Escherichia coli strain BL21 Star (DE3) pLysS	Bacillus anthracis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme BaP4H complexed with cadmium or 2-oxoglutarate, mixing of 0.001 ml of 9 mg/ml protein solution containing 1 mM CoCl2 and 1 mM 2-oxoglutarate with 0.001 ml of reservoir solution containing 0.1 M HEPES, pH 7.8, 0.05 M cadmium sulfate, and 0.9 M sodium acetate, equilibration against 0.35 ml of reservoir solution, at 20°C, X-ray diffraction structure determination and analysis at 1.63 and 2.35 A resolution, respectively, soaking of the different crystals in different cryoprotection solutions, molecular replacement using the monomer (chain A), PDB Id 3itq, as a starting model	Bacillus anthracis

Crystallization (Comment)

Organism

purified enzyme BaP4H complexed with cadmium or 2-oxoglutarate, mixing of 0.001 ml of 9 mg/ml protein solution containing 1 mM CoCl2 and 1 mM 2-oxoglutarate with 0.001 ml of reservoir solution containing 0.1 M HEPES, pH 7.8, 0.05 M cadmium sulfate, and 0.9 M sodium acetate, equilibration against 0.35 ml of reservoir solution, at 20°C, X-ray diffraction structure determination and analysis at 1.63 and 2.35 A resolution, respectively, soaking of the different crystals in different cryoprotection solutions, molecular replacement using the monomer (chain A), PDB Id 3itq, as a starting model

Bacillus anthracis

Inhibitors

Inhibitors	Comment	Organism	Structure
Cd2+	the binding of Cd2+ induces a conformational change in the enzyme structure compared to the wild-type enzyme, overview	Bacillus anthracis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	a non-heme iron enzyme, required for catalysis	Bacillus anthracis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
procollagen L-proline + 2-oxoglutarate + O2	Bacillus anthracis	-	procollagen trans-4-hydroxy-L-proline + succinate + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus anthracis	Q81LZ8	alpha-subunit domain protein	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from by a process involving hydrophobic interaction chromatography purification step prior to gel filtration	Bacillus anthracis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
procollagen L-proline + 2-oxoglutarate + O2	-	Bacillus anthracis	procollagen trans-4-hydroxy-L-proline + succinate + CO2	-	?

Synonyms

Synonyms	Comment	Organism
BaP4H	-	Bacillus anthracis
GBAA_4459	-	Bacillus anthracis
P4H	-	Bacillus anthracis
prolyl 4-hydroxylase	-	Bacillus anthracis

General Information

General Information	Comment	Organism
metabolism	the stabilization of collagen triple-helical structure via prolyl hydroxylation involving the enzyme is the rate-limiting step in collagen biosynthesis	Bacillus anthracis
additional information	active site structure and substrate recognition, overview	Bacillus anthracis
physiological function	prolyl 4-hydroxylases are mononuclear nonheme iron enzymes that catalyze the formation of 4R-hydroxyproline from many different substrates, with various biological implications. P4H is a key player in collagen accumulation. The stabilization of collagen triple-helical structure via prolyl hydroxylation is the rate-limiting step in collagen biosynthesis	Bacillus anthracis