1wb8
From Proteopedia
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| - | [[Image:1wb8.png|left|200px]] | ||
| - | < | + | ==Iron Superoxide Dismutase (FE-SOD) from the Hyperthermophile SULFOLOBUS SOLFATARICUS. 2.3 A Resolution Structure of Recombinant Protein with a Covalently Modified Tyrosine in the Active Site.== |
| - | + | <StructureSection load='1wb8' size='340' side='right'caption='[[1wb8]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[1wb8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sss 1sss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WB8 FirstGlance]. <br> | |
| - | or | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | -- | + | <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>, <scene name='pdbligand=PMS:PHENYLMETHANESULFONIC+ACID'>PMS</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=1wb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wb8 OCA], [https://pdbe.org/1wb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wb8 RCSB], [https://www.ebi.ac.uk/pdbsum/1wb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wb8 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SODF_SACS2 SODF_SACS2] 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/wb/1wb8_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=1wb8 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure of superoxide dismutase (SOD) from the hyper thermophile Sulfolobus solfataricus has been determined at 2.3 A resolution by molecular replacement and refined to a crystallographic R-factor of 16.8 % (Rfree 19.8 %). The crystals belong to the space group C2 (a=76.3 A, b=124.3 A, c=60.3 A, beta=128.8 degrees) with two identical monomers in the asymmetric unit. The monomer has a molecular weight of 24 kDa and consists of 210 amino acid residues of which 205 are visible in the electron density map. The overall fold of the monomer of S. solfataricus SOD is similar to that of the other known Fe or Mn-SODs. S. solfataricus SOD forms a very compact tetramer of a type similar to that of SOD from the hyperthermophile Aquifex pyrophilus. Both structures show an elevated number of inter-subunit ion-pairs compared with the mesophilic SOD from Mycobacterium tuberculosis and the thermophilic SOD from Thermus thermophilus. However, in contrast to the A. pyrophilus SOD structure, the number of intra-subunit ion-pairs as well as inter- subunit hydrogen bonds is not higher than in the compared mesophilic and thermophilic SOD structures. The electron density also revealed an unexpected and unusual covalent modification of a conserved tyrosine in the active site. Its involvement in the specific activity of the enzyme is discussed. | ||
| - | + | Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: analysis of structure and thermostability.,Ursby T, Adinolfi BS, Al-Karadaghi S, De Vendittis E, Bocchini V J Mol Biol. 1999 Feb 12;286(1):189-205. PMID:9931259<ref>PMID:9931259</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1wb8" style="background-color:#fffaf0;"></div> | |
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| - | == | + | |
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==See Also== | ==See Also== | ||
| - | *[[Superoxide | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Adinolfi | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Al-Karadaghi | + | [[Category: Adinolfi BS]] |
| - | [[Category: Bocchini | + | [[Category: Al-Karadaghi S]] |
| - | + | [[Category: Bocchini V]] | |
| - | [[Category: Vendittis | + | [[Category: De Vendittis E]] |
| - | [[Category: | + | [[Category: Ursby T]] |
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Current revision
Iron Superoxide Dismutase (FE-SOD) from the Hyperthermophile SULFOLOBUS SOLFATARICUS. 2.3 A Resolution Structure of Recombinant Protein with a Covalently Modified Tyrosine in the Active Site.
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