1ogp
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The molybdenum cofactor (Moco) containing sulfite oxidase (SO) from | + | 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== | ||
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[[Category: Fischer, K.]] | [[Category: Fischer, K.]] | ||
[[Category: Kisker, C.]] | [[Category: Kisker, C.]] | ||
| - | [[Category: Mendel, R | + | [[Category: Mendel, R R.]] |
[[Category: Schrader, N.]] | [[Category: Schrader, N.]] | ||
[[Category: Schwarz, G.]] | [[Category: Schwarz, G.]] | ||
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[[Category: plant sulfite oxidase]] | [[Category: plant sulfite oxidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:34 2008'' |
Revision as of 12:17, 21 February 2008
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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 with , and as ligands. Active as Sulfite oxidase, with EC number 1.8.3.1 Known structural/functional Site: . 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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