2rcv
From Proteopedia
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(New page: 200px<br /><applet load="2rcv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2rcv, resolution 1.60Å" /> '''Crystal structure of...) |
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| - | [[Image:2rcv.jpg|left|200px]]<br /><applet load="2rcv" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2rcv, resolution 1.60Å" /> | ||
| - | '''Crystal structure of the Bacillus subtilis superoxide dismutase'''<br /> | ||
| - | == | + | ==Crystal structure of the Bacillus subtilis superoxide dismutase== |
| + | <StructureSection load='2rcv' size='340' side='right'caption='[[2rcv]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2rcv]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RCV 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]] 1.6Å</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=2rcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rcv OCA], [https://pdbe.org/2rcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rcv RCSB], [https://www.ebi.ac.uk/pdbsum/2rcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rcv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SODM_BACSU SODM_BACSU] 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/rc/2rcv_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=2rcv ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The sodA gene of Bacillus subtilis was expressed in Escherichia coli, purified and crystallized. The crystal structure of MnSOD was solved by molecular replacement with four dimers per asymmetric unit and refined to an R factor of 21.1% at 1.8 A resolution. The dimer structure is very similar to that of the related enzyme from B. anthracis. Larger structural differences were observed with the human MnSOD, which has one less helix in the helical domain and a longer loop between two beta-strands and also showed differences in three amino acids at the intersubunit interface in the dimer compared with the two bacterial MnSODs. These structural differences can be exploited in the design of drugs that selectively target the Bacillus enzymes. | The sodA gene of Bacillus subtilis was expressed in Escherichia coli, purified and crystallized. The crystal structure of MnSOD was solved by molecular replacement with four dimers per asymmetric unit and refined to an R factor of 21.1% at 1.8 A resolution. The dimer structure is very similar to that of the related enzyme from B. anthracis. Larger structural differences were observed with the human MnSOD, which has one less helix in the helical domain and a longer loop between two beta-strands and also showed differences in three amino acids at the intersubunit interface in the dimer compared with the two bacterial MnSODs. These structural differences can be exploited in the design of drugs that selectively target the Bacillus enzymes. | ||
| - | + | Structure of Bacillus subtilis superoxide dismutase.,Liu P, Ewis HE, Huang YJ, Lu CD, Tai PC, Weber IT Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Dec 1;63(Pt, 12):1003-7. Epub 2007 Nov 21. PMID:18084079<ref>PMID:18084079</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2rcv" 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 subtilis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ewis HE]] | ||
| + | [[Category: Huang YJ]] | ||
| + | [[Category: Liu P]] | ||
| + | [[Category: Lu CD]] | ||
| + | [[Category: Tai PC]] | ||
| + | [[Category: Weber IT]] | ||
Current revision
Crystal structure of the Bacillus subtilis superoxide dismutase
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Categories: Bacillus subtilis | Large Structures | Ewis HE | Huang YJ | Liu P | Lu CD | Tai PC | Weber IT
