1sp8: Difference between revisions
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'''4-Hydroxyphenylpyruvate Dioxygenase''' | {{Structure | ||
|PDB= 1sp8 |SIZE=350|CAPTION= <scene name='initialview01'>1sp8</scene>, resolution 2.Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FE2:FE (II) ION'>FE2</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''4-Hydroxyphenylpyruvate Dioxygenase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SP8 is a [ | 1SP8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP8 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15084729 15084729] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:07:54 2008'' | ||
Revision as of 15:07, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
4-Hydroxyphenylpyruvate Dioxygenase
OverviewOverview
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 StructureAbout this Structure
1SP8 is a Protein complex structure of sequences from Zea mays. Full crystallographic information is available from OCA.
ReferenceReference
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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