1to5
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(New page: 200px<br /><applet load="1to5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1to5, resolution 2.20Å" /> '''Structure of the cyt...)
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Revision as of 01:20, 21 November 2007
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Structure of the cytosolic Cu,Zn SOD from S. mansoni
Overview
Cu,Zn superoxide dismutase (Cu,Zn SOD) is an essential enzyme for, protecting cells from the toxic effects of reactive oxygen species. In, humans, two distinct Cu,Zn SOD genes are located on chromosomes 4 and 21, and mutations in the latter have been associated with familial amyotrophic, lateral sclerosis. Similarly, schistosomes (trematode parasites, responsible for the chronically debilitating disease schistosomiasis) also, produce two distinct Cu,Zn SODs, in this case one cytosolic and one, bearing a signal peptide. The crystal structure of the cytosolic form of, the enzyme from the human trematode Schistosoma mansoni (SmCtSOD) was, solved and refined to a resolution of 2.2 A (space group P2(1)2(1)2(1), R, = 17.6% and R(free) = 24.1%) and 1.55 A (space group P2(1), R = 15.7% and, R(free) = 17.1%). This is the first report of a crystal structure of a, Cu,Zn superoxide dismutase derived from a human parasite. Alternate, positions for the catalytic copper and its water ligand were refined for, the 1.55 A SmCtSOD model, but the most interesting structural differences, between SmCtSOD and the human homologue reside in the loops used for, electrostatic guidance of the substrate to the enzyme active site.
About this Structure
1TO5 is a Single protein structure of sequence from Schistosoma mansoni with ZN, CU and ACT as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.
Reference
Structure of the cytosolic Cu,Zn superoxide dismutase from Schistosoma mansoni., Cardoso RM, Silva CH, Ulian de Araujo AP, Tanaka T, Tanaka M, Garratt RC, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1569-78. Epub 2004, Aug 26. PMID:15333927
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