Crystallization (Comment) | Organism |
---|---|
purified SeMet anthrax P4H, hanging drop vapor diffusion method, 24 mg/mL protein in 50 mM Tris, pH 7.4, containing 150 mM KCl and 5 mM 2-mercaptoethanol, is mixed with and equal volume of well solution containing 16% w/v PEG 8000, 40 mM potassium phosphate, pH 4.0-4.2, and 20% v/v glycerol, at 20°C, under aerobic conditions, 1-2 weeks, X-ray diffraction structure determination and analysis at 1.4 A resolution | Bacillus anthracis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | required for activity, binds in a conserved facial triad binding site, His1-X-Asp/Glu-Xn-His2 | Bacillus anthracis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(Gly-Pro-Pro)10 + 2-oxoglutarate + O2 | Bacillus anthracis | - |
? | - |
? | |
procollagen L-proline + 2-oxoglutarate + O2 | Bacillus anthracis | - |
procollagen trans-4-hydroxy-L-proline + succinate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | Q81LZ8 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(Gly-Pro-Pro)10 + 2-oxoglutarate + O2 | - |
Bacillus anthracis | ? | - |
? | |
procollagen L-proline + 2-oxoglutarate + O2 | - |
Bacillus anthracis | procollagen trans-4-hydroxy-L-proline + succinate + CO2 | - |
? | |
procollagen L-proline + 2-oxoglutarate + O2 | substrate binding and active site structure, overview | Bacillus anthracis | procollagen trans-4-hydroxy-L-proline + succinate + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme possesses the double-stranded beta-helix core fold characteristic of Fe(II)/2-oxoglutarate oxygenases, that positions Fe-binding and 2-oxoglutarate-binding residues in what is expected to be catalytically competent orientations and is consistent with proline peptide substrate binding at the active site mouth | Bacillus anthracis |
Synonyms | Comment | Organism |
---|---|---|
P4H | - |
Bacillus anthracis |
prolyl 4-hydroxylase | - |
Bacillus anthracis |
General Information | Comment | Organism |
---|---|---|
physiological function | prolyl 4-hydroxylase catalyzes the post-translational hydroxylation of proline residues and plays a role in collagen production, hypoxia response, and cell wall development | Bacillus anthracis |