1my6
From Proteopedia
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<StructureSection load='1my6' size='340' side='right'caption='[[1my6]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1my6' size='340' side='right'caption='[[1my6]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1my6]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1my6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus Thermosynechococcus vestitus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MY6 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]] 1.6Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1my6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1my6 OCA], [https://pdbe.org/1my6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1my6 RCSB], [https://www.ebi.ac.uk/pdbsum/1my6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1my6 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/Q8DIR2_THEVB Q8DIR2_THEVB] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] |
== 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=1my6 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=1my6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The iron-containing superoxide dismutase (FeSOD) from the thermophilic cyanobacterium Thermosynechococcus elongatus has been isolated. The protein crystallizes readily and we have determined the structure to 1.6 A resolution. This is the first structural characterization of an FeSOD isolated from a cyanobacterium and one of the highest resolution FeSOD structures determined to date. The activity of the T. elongatus FeSOD has been measured both at 25 degrees C and 50 degrees C and it has been spectroscopically characterized. The T. elongatus FeSOD EPR spectra at pH 5.1, 7.5 and 10.0 are similar. This indicates that no change in the geometry of the Fe(III) site occurs over a wide range of pH. This is in contrast to the other FeSODs described in the literature. | ||
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- | The 1.6 A resolution structure of Fe-superoxide dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus.,Kerfeld CA, Yoshida S, Tran KT, Yeates TO, Cascio D, Bottin H, Berthomieu C, Sugiura M, Boussac A J Biol Inorg Chem. 2003 Sep;8(7):707-14. Epub 2003 Jun 24. PMID:12827458<ref>PMID:12827458</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1my6" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
- | *[[Superoxide | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | + | [[Category: Thermosynechococcus vestitus]] | |
- | [[Category: Thermosynechococcus | + | [[Category: Cascio D]] |
- | [[Category: Cascio | + | [[Category: Kerfeld CA]] |
- | [[Category: Kerfeld | + | [[Category: Sawaya MR]] |
- | [[Category: Sawaya | + | [[Category: Yeates TO]] |
- | [[Category: Yeates | + | [[Category: Yoshida SM]] |
- | [[Category: Yoshida | + | |
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Current revision
The 1.6 A Structure of Fe-Superoxide Dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus : Correlation of EPR and Structural Characteristics
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