PDBsum entry: 1cjx

Oxidoreductase

PDB id: 1cjx

Contents

Protein chains

353 a.a. *

Ligands

EMC ×4

ACT ×4

Metals

FE2 ×4

Waters ×567

* Residue conservation analysis

PDB id:

1cjx

Name:

Oxidoreductase

Title:

Crystal structure of pseudomonas fluorescens hppd

Structure:

4-hydroxyphenylpyruvate dioxygenase. Chain: a, b, c, d. Engineered: yes

Source:

Pseudomonas fluorescens. Organism_taxid: 294. Cell_line: a32. Expressed in: pseudomonas fluorescens. Expression_system_taxid: 294. Expression_system_cell_line: a32.

Biol. unit:

Dimer (from PQS)

Resolution:

2.40Å R-factor: 0.219 R-free: 0.276

Authors:

L.Serre,A.Sailland,D.Sy,P.Boudec,A.Rolland,E.Pebay-Peroulla, C.Cohen-Addad

Key ref:

L.Serre et al. (1999). Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway. Structure, 7, 977-988. PubMed id: 10467142 DOI: 10.1016/S0969-2126(99)80124-5

Date:

20-Apr-99 Release date: 26-Apr-00

Protein chains

P80064  (HPPD_PSEUJ) -  4-hydroxyphenylpyruvate dioxygenase

Seq: 357 a.a.

Struc: 353 a.a.*

* PDB and UniProt seqs differ at 25 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.1.13.11.27 - 4-hydroxyphenylpyruvate dioxygenase.
• Reaction: 4-hydroxyphenylpyruvate + O₂ = homogentisate + CO₂

4-hydroxyphenylpyruvate + O(2) = homogentisate + CO(2) (Bound ligand (Het Group name = ACT) matches with 75.00% similarity)

• Cofactor: Iron

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: oxidation-reduction process (4 terms)
• Biochemical function: oxidoreductase activity (5 terms)

reference

DOI no: 10.1016/S0969-2126(99)80124-5

Structure 7:977-988 (1999)

PubMed id: 10467142

Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway.

L.Serre, A.Sailland, D.Sy, P.Boudec, A.Rolland, E.Pebay-Peyroula, C.Cohen-Addad.

ABSTRACT

BACKGROUND: 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. RESULTS: We report here the crystal structure of Pseudomonas fluorescens HPPD refined to 2.4 A resolution (Rfree 27.6%; R factor 21.9%). The general topology of the protein comprises two barrel-shaped domains and is similar to the structures of Pseudomonas 2,3-dihydroxybiphenyl dioxygenase (DHBD) and Pseudomonas putida catechol 2,3-dioxygenase (MPC). Each structural domain contains two repeated betaalpha betabeta betaalpha modules. There is one non-heme iron atom per monomer liganded to the sidechains of His161, His240, Glu322 and one acetate molecule. CONCLUSIONS: The analysis of the HPPD structure and its superposition with the structures of DHBD and MPC highlight some important differences in the active sites of these enzymes. These comparisons also suggest that the pyruvate part of the HPPD substrate (4-hydroxyphenylpyruvate) and the O2 molecule would occupy the three free coordination sites of the catalytic iron atom. This substrate-enzyme model will aid the design of new inhibitors of the homogentisate biosynthesis reaction.

Selected figure(s)

Figure 1.
Figure 1. Homogentisate biosynthesis. Schematic of the reaction catalyzed by HPPD.

The above figure is reprinted by permission from Cell Press: Structure (1999, 7, 977-988) copyright 1999.

Figure was selected by an automated process.