1sp9

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{{STRUCTURE_1sp9| PDB=1sp9 | SCENE= }}
{{STRUCTURE_1sp9| PDB=1sp9 | SCENE= }}
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'''4-Hydroxyphenylpyruvate Dioxygenase'''
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===4-Hydroxyphenylpyruvate Dioxygenase===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15084729}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15084729 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15084729}}
==About this Structure==
==About this Structure==
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[[Category: Steinbacher, S.]]
[[Category: Steinbacher, S.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:58:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:24:04 2008''

Revision as of 04:24, 29 July 2008

Image:1sp9.png

Template:STRUCTURE 1sp9

4-Hydroxyphenylpyruvate Dioxygenase

Template:ABSTRACT PUBMED 15084729

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

Page seeded by OCA on Tue Jul 29 07:24:04 2008

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