5ag2: Difference between revisions
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==SOD-3 azide complex== | ==SOD-3 azide complex== | ||
<StructureSection load='5ag2' size='340' side='right' caption='[[5ag2]], [[Resolution|resolution]] 1.77Å' scene=''> | <StructureSection load='5ag2' size='340' side='right'caption='[[5ag2]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ag2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AG2 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5ag2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AG2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77Å</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=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5ag2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ag2 OCA], [https://pdbe.org/5ag2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ag2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ag2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ag2 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SODM2_CAEEL SODM2_CAEEL] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 19: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5ag2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ag2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Caenorhabditis elegans]] | ||
[[Category: Bonetta | [[Category: Large Structures]] | ||
[[Category: Cabelli | [[Category: Bonetta R]] | ||
[[Category: Hunter | [[Category: Cabelli DE]] | ||
[[Category: Hunter | [[Category: Hunter GJ]] | ||
[[Category: Stewart | [[Category: Hunter T]] | ||
[[Category: Trinh | [[Category: Stewart EE]] | ||
[[Category: Trinh CH]] | |||
Latest revision as of 14:08, 10 January 2024
SOD-3 azide complexSOD-3 azide complex
Structural highlights
FunctionSODM2_CAEEL Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Publication Abstract from PubMedC. elegans MnSOD-3 has been implicated in the longevity pathway and its mechanism of catalysis is relevant to the aging process and carcinogenesis. The structures of MnSOD-3 provide unique crystallographic evidence of a dynamic region of the tetrameric interface (residues 41-54). We have determined the structure of the MnSOD-3-azide complex to 1.77-A resolution. Analysis of this complex shows that the substrate analog, azide, binds end-on to the manganese center as a sixth ligand and that it ligates directly to a third and new solvent molecule also positioned within interacting distance to the His30 and Tyr34 residues of the substrate access funnel. This is the first structure of a eukaryotic MnSOD-azide complex that demonstrates the extended, uninterrupted hydrogen-bonded network that forms a proton relay incorporating three outer sphere solvent molecules, the substrate analog, the gateway residues, Gln142, and the solvent ligand. This configuration supports the formation and release of the hydrogen peroxide product in agreement with the 5-6-5 catalytic mechanism for MnSOD. The high product dissociation constant k4 of MnSOD-3 reflects low product inhibition making this enzyme efficient even at high levels of superoxide. The structure of the Caenorhabditis elegans manganese superoxide dismutase MnSOD-3-azide complex.,Hunter GJ, Trinh CH, Bonetta R, Stewart EE, Cabelli DE, Hunter T Protein Sci. 2015 Nov;24(11):1777-88. doi: 10.1002/pro.2768. Epub 2015 Aug 27. PMID:26257399[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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