1xre
From Proteopedia
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| - | [[Image:1xre.gif|left|200px]]<br /><applet load="1xre" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1xre, resolution 1.80Å" /> | ||
| - | '''Crystal Structure of SodA-2 (BA5696) from Bacillus anthracis at 1.8A Resolution.'''<br /> | ||
| - | == | + | ==Crystal Structure of SodA-2 (BA5696) from Bacillus anthracis at 1.8A Resolution.== |
| + | <StructureSection load='1xre' size='340' side='right'caption='[[1xre]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1xre]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XRE FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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></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=1xre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xre OCA], [https://pdbe.org/1xre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xre RCSB], [https://www.ebi.ac.uk/pdbsum/1xre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xre ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SODM2_BACAN SODM2_BACAN] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xr/1xre_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1xre ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The BA4499 and BA5696 genes of Bacillus anthracis encode proteins homologous to manganese superoxide dismutase, suggesting that this organism has an expanded repertoire of antioxidant proteins. Differences in metal specificity and quaternary structure between the dismutases of prokaryotes and higher eukaryotes may be exploited in the development of therapeutic antibacterial compounds. Here, the crystal structure of two Mn superoxide dismutases from B. anthracis solved to high resolution are reported. Comparison of their structures reveals that a highly conserved residue near the active centre is substituted in one of the proteins and that this is a characteristic feature of superoxide dismutases from the B. cereus/B. anthracis/B. thuringiensis group of organisms. | The BA4499 and BA5696 genes of Bacillus anthracis encode proteins homologous to manganese superoxide dismutase, suggesting that this organism has an expanded repertoire of antioxidant proteins. Differences in metal specificity and quaternary structure between the dismutases of prokaryotes and higher eukaryotes may be exploited in the development of therapeutic antibacterial compounds. Here, the crystal structure of two Mn superoxide dismutases from B. anthracis solved to high resolution are reported. Comparison of their structures reveals that a highly conserved residue near the active centre is substituted in one of the proteins and that this is a characteristic feature of superoxide dismutases from the B. cereus/B. anthracis/B. thuringiensis group of organisms. | ||
| - | + | Structures of two superoxide dismutases from Bacillus anthracis reveal a novel active centre.,Boucher IW, Kalliomaa AK, Levdikov VM, Blagova EV, Fogg MJ, Brannigan JA, Wilson KS, Wilkinson AJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt, 7):621-4. Epub 2005 Jun 15. PMID:16511113<ref>PMID:16511113</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1xre" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus anthracis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Blagova EV]] | ||
| + | [[Category: Boucher IW]] | ||
| + | [[Category: Brannigan JA]] | ||
| + | [[Category: Fogg MJ]] | ||
| + | [[Category: Levdikov VM]] | ||
| + | [[Category: Wilkinson AJ]] | ||
| + | [[Category: Wilson KS]] | ||
Current revision
Crystal Structure of SodA-2 (BA5696) from Bacillus anthracis at 1.8A Resolution.
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