1to5

<table><tr><td colspan='2'>[[1to5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TO5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TO5 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1to4|1to4]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SOD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6183 Blood fluke])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1to5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1to5 OCA], [http://pdbe.org/1to5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1to5 RCSB], [http://www.ebi.ac.uk/pdbsum/1to5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1to5 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SODC_SCHMA SODC_SCHMA]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15333927</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1to5" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Blood fluke]]

[[Category: Superoxide dismutase]]

[[Category: Araujo, A P.Ulian de]]

[[Category: Cardoso, R M.F]]

[[Category: Garratt, R C]]

[[Category: Silva, C H.T P]]

[[Category: Tanaka, M]]

[[Category: Tanaka, T]]

[[Category: Beta-barrel]]

[[Category: Oxidoreductase]]