1CJX
CRYSTAL STRUCTURE OF PSEUDOMONAS FLUORESCENS HPPD
Summary for 1CJX
| Entry DOI | 10.2210/pdb1cjx/pdb |
| Descriptor | 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE, FE (II) ION, ETHYL MERCURY ION, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, dioxygenase, iron |
| Biological source | Pseudomonas fluorescens |
| Total number of polymer chains | 4 |
| Total formula weight | 161755.85 |
| Authors | Serre, L.,Sailland, A.,Sy, D.,Boudec, P.,Rolland, A.,Pebay-Peroulla, E.,Cohen-Addad, C. (deposition date: 1999-04-20, release date: 2000-04-26, Last modification date: 2023-12-27) |
| Primary citation | Serre, L.,Sailland, A.,Sy, D.,Boudec, P.,Rolland, A.,Pebay-Peyroula, E.,Cohen-Addad, C. Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway. Structure Fold.Des., 7:977-988, 1999 Cited by PubMed Abstract: In plants and photosynthetic bacteria, the tyrosine degradation pathway is crucial because homogentisate, a tyrosine degradation product, is a precursor for the biosynthesis of photosynthetic pigments, such as quinones or tocophenols. Homogentisate biosynthesis includes a decarboxylation step, a dioxygenation and a rearrangement of the pyruvate sidechain. This complex reaction is carried out by a single enzyme, the 4-hydroxyphenylpyruvate dioxygenase (HPPD), a non-heme iron dependent enzyme that is active as a homotetramer in bacteria and as a homodimer in plants. Moreover, in humans, a HPPD deficiency is found to be related to tyrosinemia, a rare hereditary disorder of tyrosine catabolism. PubMed: 10467142DOI: 10.1016/S0969-2126(99)80124-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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