3dc6

<StructureSection load='3dc6' size='340' side='right' caption='[[3dc6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[3dc6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DC6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dc5|3dc5]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sod-2, sdm-1, F10D11.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dc6 OCA], [http://pdbe.org/3dc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dc6 RCSB], [http://www.ebi.ac.uk/pdbsum/3dc6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dc6 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SODM1_CAEEL SODM1_CAEEL]] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

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== Publication Abstract from PubMed ==

Caenorhabditis elegans expresses two manganese superoxide dismutase enzymes (MnSOD-2 and MnSOD-3) that are targeted to the mitochondrion. MnSOD-2 is constitutively expressed, while synthesis of MnSOD-3 is inducible. The structures of these two mononuclear metalloenzymes have been determined to 1.8 and 1.7 A resolution, respectively. Pink crystals formed in space group P4(1)2(1)2 for each, with unit-cell parameters a = b = 81.0, c = 137.4 A for MnSOD-2 and a = b = 81.8, c = 136.0 A for MnSOD-3. The final structure of MnSOD-3 was refined to R = 21.6% and R(free) = 26.2% at 293 K, and R = 18.9% and R(free) = 22.6% at 100 K, while that of MnSOD-2 was refined to R = 16.9% and R(free) = 20.1% at 100 K. The asymmetric unit cell is comprised of two subunits. The resulting structures are very similar to that of human MnSOD and form a tetramer corresponding to a dimer of dimers. The subunit interface between dimers is comprised of two four-helix bundles that stabilize the biologically significant homotetramer.

Purification, crystallization and X-ray structures of the two manganese superoxide dismutases from Caenorhabditis elegans.,Trinh CH, Hunter T, Stewart EE, Phillips SE, Hunter GJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Dec 1;64(Pt, 12):1110-4. Epub 2008 Nov 28. PMID:19052361<ref>PMID:19052361</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 3dc6" style="background-color:#fffaf0;"></div>

*[[Superoxide Dismutase|Superoxide Dismutase]]

[[Category: Caeel]]

[[Category: Superoxide dismutase]]

[[Category: Hunter, G J]]

[[Category: Hunter, T]]

[[Category: Phillips, S E.V]]

[[Category: Stewart, E E]]

[[Category: Trinh, C H]]

[[Category: Transit peptide]]