1sp9
From Proteopedia
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|PDB= 1sp9 |SIZE=350|CAPTION= <scene name='initialview01'>1sp9</scene>, resolution 3.Å | |PDB= 1sp9 |SIZE=350|CAPTION= <scene name='initialview01'>1sp9</scene>, resolution 3.Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FE2:FE (II) ION'>FE2</scene> | + | |LIGAND= <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= HPD, AT1G06570, F12K11.9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | |GENE= HPD, AT1G06570, F12K11.9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1sp8|1SP8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sp9 OCA], [http://www.ebi.ac.uk/pdbsum/1sp9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sp9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Linden, L.]] | [[Category: Linden, L.]] | ||
[[Category: Steinbacher, S.]] | [[Category: Steinbacher, S.]] | ||
| - | [[Category: FE2]] | ||
[[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 23:45:14 2008'' |
Revision as of 20:45, 30 March 2008
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| , resolution 3.Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | HPD, AT1G06570, F12K11.9 (Arabidopsis thaliana) | ||||||
| Activity: | 4-hydroxyphenylpyruvate dioxygenase, with EC number 1.13.11.27 | ||||||
| Related: | 1SP8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
4-Hydroxyphenylpyruvate Dioxygenase
Overview
The transformation of 4-hydroxyphenylpyruvate to homogentisate, catalyzed by 4-hydroxyphenylpyruvate dioxygenase (HPPD), plays an important role in degrading aromatic amino acids. As the reaction product homogentisate serves as aromatic precursor for prenylquinone synthesis in plants, the enzyme is an interesting target for herbicides. In this study we report the first x-ray structures of the plant HPPDs of Zea mays and Arabidopsis in their substrate-free form at 2.0 A and 3.0 A resolution, respectively. Previous biochemical characterizations have demonstrated that eukaryotic enzymes behave as homodimers in contrast to prokaryotic HPPDs, which are homotetramers. Plant and bacterial enzymes share the overall fold but use orthogonal surfaces for oligomerization. In addition, comparison of both structures provides direct evidence that the C-terminal helix gates substrate access to the active site around a nonheme ferrous iron center. In the Z. mays HPPD structure this helix packs into the active site, sequestering it completely from the solvent. In contrast, in the Arabidopsis structure this helix tilted by about 60 degrees into the solvent and leaves the active site fully accessible. By elucidating the structure of plant HPPD enzymes we aim to provide a structural basis for the development of new herbicides.
About this Structure
1SP9 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase., Fritze IM, Linden L, Freigang J, Auerbach G, Huber R, Steinbacher S, Plant Physiol. 2004 Apr;134(4):1388-400. PMID:15084729
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