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| | <StructureSection load='1jr9' size='340' side='right'caption='[[1jr9]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1jr9' size='340' side='right'caption='[[1jr9]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1jr9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Virgibacillus_halodenitrificans Virgibacillus halodenitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JR9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JR9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1jr9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Virgibacillus_halodenitrificans Virgibacillus halodenitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JR9 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=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1jr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jr9 OCA], [http://pdbe.org/1jr9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jr9 RCSB], [http://www.ebi.ac.uk/pdbsum/1jr9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jr9 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jr9 OCA], [https://pdbe.org/1jr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jr9 RCSB], [https://www.ebi.ac.uk/pdbsum/1jr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jr9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SODM_VIRHA SODM_VIRHA]] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Active only in homodimeric state.<ref>PMID:12457847</ref> | + | [https://www.uniprot.org/uniprot/SODM_VIRHA SODM_VIRHA] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Active only in homodimeric state.<ref>PMID:12457847</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Superoxide Dismutase|Superoxide Dismutase]] | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Superoxide dismutase]] | |
| | [[Category: Virgibacillus halodenitrificans]] | | [[Category: Virgibacillus halodenitrificans]] |
| - | [[Category: Chang, T]] | + | [[Category: Chang T]] |
| - | [[Category: Chang, W R]] | + | [[Category: Chang WR]] |
| - | [[Category: Gui, L L]] | + | [[Category: Gui LL]] |
| - | [[Category: Jiang, T]] | + | [[Category: Jiang T]] |
| - | [[Category: LeGall, J]] | + | [[Category: LeGall J]] |
| - | [[Category: Li, M]] | + | [[Category: Li M]] |
| - | [[Category: Liang, D C]] | + | [[Category: Liang DC]] |
| - | [[Category: Liao, J]] | + | [[Category: Liao J]] |
| - | [[Category: Liu, M Y]] | + | [[Category: Liu MY]] |
| - | [[Category: Zhang, J P]] | + | [[Category: Zhang JP]] |
| - | [[Category: Manganese superoxide dismutase]]
| + | |
| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
SODM_VIRHA Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Active only in homodimeric state.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A so-called "green protein" has been purified from a moderate halophilic eubacterium, Bacillus halodenitrificans (ATCC 49067), under anaerobic conditions. The protein, which might play an important role in denitrification, dissociates mainly into two components after exposure to air: a manganese superoxide dismutase (GP-MnSOD) and a nucleoside diphosphate kinase. As a first step in elucidating the overall structure of the green protein and the role of each component, the 2.8-A resolution crystal structure of GP-MnSOD was determined. Compared with other manganese dismutases, GP-MnSOD shows two significant characteristics. The first is that the entrance to its substrate channel has an additional basic residue-Lys38. The second is that its surface is decorated with an excess of acidic over basic residues. All these structural features may be related to GP-MnSOD's high catalytic activity and its endurance against the special cytoplasm of B. halodenitrificans. The structure of GP-MnSOD provides the basis for recognizing its possible role and assembly state in the green protein.
Three-dimensional structure of manganese superoxide dismutase from Bacillus halodenitrificans, a component of the so-called "green protein".,Liao J, Liu MY, Chang T, Li M, Le Gall J, Gui LL, Zhang JP, Jiang T, Liang DC, Chang WR J Struct Biol. 2002 Sep;139(3):171-80. PMID:12457847[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liao J, Liu MY, Chang T, Li M, Le Gall J, Gui LL, Zhang JP, Jiang T, Liang DC, Chang WR. Three-dimensional structure of manganese superoxide dismutase from Bacillus halodenitrificans, a component of the so-called "green protein". J Struct Biol. 2002 Sep;139(3):171-80. PMID:12457847
- ↑ Liao J, Liu MY, Chang T, Li M, Le Gall J, Gui LL, Zhang JP, Jiang T, Liang DC, Chang WR. Three-dimensional structure of manganese superoxide dismutase from Bacillus halodenitrificans, a component of the so-called "green protein". J Struct Biol. 2002 Sep;139(3):171-80. PMID:12457847
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