1sp9

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[[Image:1sp9.jpg|left|200px]]
[[Image:1sp9.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1sp9 |SIZE=350|CAPTION= <scene name='initialview01'>1sp9</scene>, resolution 3.&Aring;
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The line below this paragraph, containing "STRUCTURE_1sp9", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= HPD, AT1G06570, F12K11.9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
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-->
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|DOMAIN=
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{{STRUCTURE_1sp9| PDB=1sp9 | SCENE= }}
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|RELATEDENTRY=[[1sp8|1SP8]]
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|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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}}
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'''4-Hydroxyphenylpyruvate Dioxygenase'''
'''4-Hydroxyphenylpyruvate Dioxygenase'''
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[[Category: Linden, L.]]
[[Category: Linden, L.]]
[[Category: Steinbacher, S.]]
[[Category: Steinbacher, S.]]
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[[Category: oxidoreductase]]
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[[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 Sun Mar 30 23:45:14 2008''
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Revision as of 05:58, 3 May 2008

Image:1sp9.jpg

Template:STRUCTURE 1sp9

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 Page seeded by OCA on Sat May 3 08:58:50 2008

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