1d5n
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1d5n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D5N FirstGlance]. <br> | <table><tr><td colspan='2'>[[1d5n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D5N FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <tr id=' | + | <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></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=1d5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d5n OCA], [https://pdbe.org/1d5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d5n RCSB], [https://www.ebi.ac.uk/pdbsum/1d5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d5n 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=1d5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d5n OCA], [https://pdbe.org/1d5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d5n RCSB], [https://www.ebi.ac.uk/pdbsum/1d5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d5n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/SODM_ECOLI SODM_ECOLI] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1d5n ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1d5n ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Superoxide dismutase protects organisms from potentially damaging oxygen radicals by catalyzing the disproportionation of superoxide to oxygen and hydrogen peroxide. We report the use of cryogenic temperatures to kinetically capture the sixth ligand bound to the active site of manganese superoxide dismutase (MnSOD). Synchrotron X-ray diffraction data was collected from Escherichia coli MnSOD crystals grown at pH 8.5 and cryocooled to 100 K. Structural refinement to 1.55 A resolution and close inspection of the active site revealed electron density for a sixth ligand that was interpreted to be a hydroxide ligand. The six-coordinate, distorted-octahedral geometry assumed during inhibition by hydroxide is compared to the room temperature, five-coordinate, trigonal bipyramidal active site determined with crystals grown from practically identical conditions. The gateway residues Tyr34, His30 and a tightly bound water molecule are implicated in closing-off the active site and blocking the escape route of the sixth ligand. | ||
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| - | Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase.,Borgstahl GE, Pokross M, Chehab R, Sekher A, Snell EH J Mol Biol. 2000 Mar 3;296(4):951-9. PMID:10686094<ref>PMID:10686094</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1d5n" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Borgstahl GEO]] | |
| - | [[Category: Borgstahl | + | [[Category: Chehab R]] |
| - | [[Category: Chehab | + | [[Category: Pokross M]] |
| - | [[Category: Pokross | + | [[Category: Sekher A]] |
| - | [[Category: Sekher | + | [[Category: Snell EH]] |
| - | [[Category: Snell | + | |
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Current revision
CRYSTAL STRUCTURE OF E. COLI MNSOD AT 100K
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