7kku
From Proteopedia
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==X-ray Counterpart to Neutron Structure of Oxidized Human MnSOD== | ==X-ray Counterpart to Neutron Structure of Oxidized Human MnSOD== | ||
| - | <StructureSection load='7kku' size='340' side='right'caption='[[7kku]]' scene=''> | + | <StructureSection load='7kku' size='340' side='right'caption='[[7kku]], [[Resolution|resolution]] 2.02Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KKU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7kku]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KKU FirstGlance]. <br> |
| - | </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=7kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kku OCA], [https://pdbe.org/7kku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kku RCSB], [https://www.ebi.ac.uk/pdbsum/7kku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kku ProSAT]</span></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]] 2.02Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN3:MANGANESE+(III)+ION'>MN3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kku OCA], [https://pdbe.org/7kku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kku RCSB], [https://www.ebi.ac.uk/pdbsum/7kku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kku ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/SODM_HUMAN SODM_HUMAN] Genetic variation in SOD2 is associated with susceptibility to microvascular complications of diabetes type 6 (MVCD6) [MIM:[https://omim.org/entry/612634 612634]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SODM_HUMAN SODM_HUMAN] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.<ref>PMID:10334867</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human manganese superoxide dismutase is a critical oxidoreductase found in the mitochondrial matrix. Concerted proton and electron transfers are used by the enzyme to rid the mitochondria of O2(*-). The mechanisms of concerted transfer enzymes are typically unknown due to the difficulties in detecting the protonation states of specific residues and solvent molecules at particular redox states. Here, neutron diffraction of two redox-controlled manganese superoxide dismutase crystals reveal the all-atom structures of Mn(3+) and Mn(2+) enzyme forms. The structures deliver direct data on protonation changes between oxidation states of the metal. Observations include glutamine deprotonation, the involvement of tyrosine and histidine with altered pKas, and four unusual strong-short hydrogen bonds, including a low barrier hydrogen bond. We report a concerted proton and electron transfer mechanism for human manganese superoxide dismutase from the direct visualization of active site protons in Mn(3+) and Mn(2+) redox states. | ||
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| + | Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase.,Azadmanesh J, Lutz WE, Coates L, Weiss KL, Borgstahl GEO Nat Commun. 2021 Apr 6;12(1):2079. doi: 10.1038/s41467-021-22290-1. PMID:33824320<ref>PMID:33824320</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7kku" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Azadmanesh J]] | [[Category: Azadmanesh J]] | ||
Current revision
X-ray Counterpart to Neutron Structure of Oxidized Human MnSOD
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