1ogp

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[[Image:1ogp.jpg|left|200px]]<br /><applet load="1ogp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ogp.jpg|left|200px]]
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caption="1ogp, resolution 2.60&Aring;" />
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'''THE CRYSTAL STRUCTURE OF PLANT SULFITE OXIDASE PROVIDES INSIGHT INTO SULFITE OXIDATION IN PLANTS AND ANIMALS'''<br />
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{{Structure
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|PDB= 1ogp |SIZE=350|CAPTION= <scene name='initialview01'>1ogp</scene>, resolution 2.60&Aring;
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|SITE= <scene name='pdbsite=AC1:Mtq+Binding+Site+For+Chain+F'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=MTQ:(MOLYBDOPTERIN-S,S)-DIOXO-THIO-MOLYBDENUM(V)'>MTQ</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Sulfite_oxidase Sulfite oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.1 1.8.3.1]
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|GENE=
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}}
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'''THE CRYSTAL STRUCTURE OF PLANT SULFITE OXIDASE PROVIDES INSIGHT INTO SULFITE OXIDATION IN PLANTS AND ANIMALS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1OGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=CS:'>CS</scene>, <scene name='pdbligand=MTQ:'>MTQ</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Sulfite_oxidase Sulfite oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.1 1.8.3.1] Known structural/functional Site: <scene name='pdbsite=AC1:Mtq+Binding+Site+For+Chain+F'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGP OCA].
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1OGP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGP OCA].
==Reference==
==Reference==
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The crystal structure of plant sulfite oxidase provides insights into sulfite oxidation in plants and animals., Schrader N, Fischer K, Theis K, Mendel RR, Schwarz G, Kisker C, Structure. 2003 Oct;11(10):1251-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14527393 14527393]
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The crystal structure of plant sulfite oxidase provides insights into sulfite oxidation in plants and animals., Schrader N, Fischer K, Theis K, Mendel RR, Schwarz G, Kisker C, Structure. 2003 Oct;11(10):1251-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14527393 14527393]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: molybdenum cofactor]]
[[Category: molybdenum cofactor]]
[[Category: molybdopterin]]
[[Category: molybdopterin]]
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[[Category: oxidoreductas]]
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[[Category: oxidoreducta]]
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[[Category: peroxisomes]]
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[[Category: peroxisome]]
[[Category: plant sulfite oxidase]]
[[Category: plant sulfite oxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:10:38 2008''

Revision as of 11:10, 20 March 2008

Image:1ogp.jpg


PDB ID 1ogp

Drag the structure with the mouse to rotate
, resolution 2.60Å
Sites:
Ligands: , and
Activity: Sulfite oxidase, with EC number 1.8.3.1
Coordinates: save as pdb, mmCIF, xml



THE CRYSTAL STRUCTURE OF PLANT SULFITE OXIDASE PROVIDES INSIGHT INTO SULFITE OXIDATION IN PLANTS AND ANIMALS


Overview

The molybdenum cofactor (Moco) containing sulfite oxidase (SO) from Arabidopsis thaliana has recently been identified and biochemically characterized. The enzyme is found in peroxisomes and believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution. Plant SO (PSO) is homodimeric and homologous to animal SO, but contains only a single Moco domain without an additional redox center. Here, we present the first crystal structure of a plant Moco enzyme, the apo-state of Arabidopsis SO at 2.6 A resolution. The overall fold and coordination of the Moco are similar to chicken SO (CSO). Comparisons of conserved surface residues and the charge distribution in PSO and CSO reveal major differences near the entrance to both active sites reflecting different electron acceptors. Arg374 has been identified as an important substrate binding residue due to its conformational change when compared to the sulfate bound structure of CSO.

About this Structure

1OGP is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

The crystal structure of plant sulfite oxidase provides insights into sulfite oxidation in plants and animals., Schrader N, Fischer K, Theis K, Mendel RR, Schwarz G, Kisker C, Structure. 2003 Oct;11(10):1251-63. PMID:14527393

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