1OGP
The crystal structure of plant sulfite oxidase provides insight into sulfite oxidation in plants and animals
Summary for 1OGP
| Entry DOI | 10.2210/pdb1ogp/pdb |
| Descriptor | SULFITE OXIDASE, CESIUM ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, molybdenum cofactor, molybdopterin, plant sulfite oxidase, peroxisomes, intramolecular electron transfer, oxidoreductas |
| Biological source | ARABIDOPSIS THALIANA (MOUSE-EAR CRESS) |
| Cellular location | Peroxisome: Q9S850 |
| Total number of polymer chains | 6 |
| Total formula weight | 265537.47 |
| Authors | Schrader, N.,Fischer, K.,Theis, K.,Mendel, R.R.,Schwarz, G.,Kisker, C. (deposition date: 2003-05-08, release date: 2003-10-09, Last modification date: 2023-12-13) |
| Primary citation | Schrader, N.,Fischer, K.,Theis, K.,Mendel, R.R.,Schwarz, G.,Kisker, C. The Crystal Structure of Plant Sulfite Oxidase Provides Insights Into Sulfite Oxidation in Plants and Animals Structure, 11:1251-, 2003 Cited by PubMed Abstract: 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. PubMed: 14527393DOI: 10.1016/J.STR.2003.09.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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