1cjx
From Proteopedia
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|PDB= 1cjx |SIZE=350|CAPTION= <scene name='initialview01'>1cjx</scene>, resolution 2.40Å | |PDB= 1cjx |SIZE=350|CAPTION= <scene name='initialview01'>1cjx</scene>, resolution 2.40Å | ||
|SITE= <scene name='pdbsite=ASA:Fe-Binding+Site'>ASA</scene>, <scene name='pdbsite=ASB:Fe-Binding+Site'>ASB</scene>, <scene name='pdbsite=ASC:Fe-Binding+Site'>ASC</scene> and <scene name='pdbsite=ASD:Fe-Binding+Site'>ASD</scene> | |SITE= <scene name='pdbsite=ASA:Fe-Binding+Site'>ASA</scene>, <scene name='pdbsite=ASB:Fe-Binding+Site'>ASB</scene>, <scene name='pdbsite=ASC:Fe-Binding+Site'>ASC</scene> and <scene name='pdbsite=ASD:Fe-Binding+Site'>ASD</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/4-hydroxyphenylpyruvate_dioxygenase 4-hydroxyphenylpyruvate dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.27 1.13.11.27] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxyphenylpyruvate_dioxygenase 4-hydroxyphenylpyruvate dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.27 1.13.11.27] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjx OCA], [http://www.ebi.ac.uk/pdbsum/1cjx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cjx RCSB]</span> | ||
}} | }} | ||
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[[Category: Serre, L.]] | [[Category: Serre, L.]] | ||
[[Category: Sy, D.]] | [[Category: Sy, D.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: EMC]] | ||
| - | [[Category: FE2]] | ||
[[Category: dioxygenase]] | [[Category: dioxygenase]] | ||
[[Category: iron]] | [[Category: iron]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:23:05 2008'' |
Revision as of 16:23, 30 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , , | ||||||
| Activity: | 4-hydroxyphenylpyruvate dioxygenase, with EC number 1.13.11.27 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PSEUDOMONAS FLUORESCENS HPPD
Overview
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.
About this Structure
1CJX is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.
Reference
Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway., Serre L, Sailland A, Sy D, Boudec P, Rolland A, Pebay-Peyroula E, Cohen-Addad C, Structure. 1999 Aug 15;7(8):977-88. PMID:10467142
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