1ogp: Difference between revisions
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==Overview== | ==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 .. | 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== | ==About this Structure== | ||
1OGP is a | 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 CS, MTQ and GOL 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OGP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: plant sulfite oxidase]] | [[Category: plant sulfite oxidase]] | ||
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Revision as of 15:58, 5 November 2007
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THE CRYSTAL STRUCTURE OF PLANT SULFITE OXIDASE PROVIDES INSIGHT INTO SULFITE OXIDATION IN PLANTS AND ANIMALS
OverviewOverview
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 StructureAbout this Structure
1OGP is a Single protein structure of sequence from Arabidopsis thaliana with CS, MTQ and GOL as ligands. Active as Sulfite oxidase, with EC number 1.8.3.1 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
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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