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1uer

From Proteopedia

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{{Seed}}
 
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[[Image:1uer.png|left|200px]]
 
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==Crystal structure of Porphyromonas gingivalis SOD==
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The line below this paragraph, containing "STRUCTURE_1uer", creates the "Structure Box" on the page.
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<StructureSection load='1uer' size='340' side='right'caption='[[1uer]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1uer]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UER FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<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>
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{{STRUCTURE_1uer| PDB=1uer | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uer OCA], [https://pdbe.org/1uer PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uer RCSB], [https://www.ebi.ac.uk/pdbsum/1uer PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uer ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SODF_PORGI SODF_PORGI] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ue/1uer_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1uer ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Glycine 155, which is located approximately 10 A from the active metal sites, is mostly conserved in aligned amino acid sequences of manganese-specific superoxide dismutases (Mn-SODs) and cambialistic SOD (showing the same activity with Fe and Mn) from Porphyromonas gingivalis, but is substituted for threonine in most Fe-SODs. Since Thr155 is located between Trp123 and Trp125, and Trp123 is one member of the metal-surrounding aromatic amino acids, there is a possibility that the conversion of this amino acid may cause a conversion of the metal-specific activity of cambialistic P. gingivalis SOD. To clarify this possibility, we have prepared a mutant of the P. gingivalis SOD with conversion of Gly155 to Thr. The ratios of the specific activities of Fe- to Mn-reconstituted enzyme, which are measured by the xanthine oxidase/cytochrome c method, increased from 0.6 in the wild-type to 11.2 in the mutant SODs, indicating the conversion of the metal-specific activity of the enzyme from a cambialistic type to an Fe-specific type. The visible absorption spectra of the Fe- and Mn-reconstituted mutant SODs closely resembled those of Fe-specific SOD. Furthermore, the EPR spectra of the Fe- and Mn-reconstituted mutant SODs also closely resembled those of Fe-specific SOD. Three-dimensional structures of the Fe-reconstituted wild-type SOD and Mn-reconstituted mutant SOD have been determined at 1.6 A resolution. Both structures have identical conformations, orientations of residues involved in metal binding, and hydrogen bond networks, while the side chain of Trp123 is moved further toward the metal-binding site than in wild-type SOD. A possible contribution of the structural differences to the conversion of the metal-specific activity through rearrangement of the hydrogen bond network among Trp123, Gln70, Tyr35, and the metal-coordinated solvent is discussed.
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===Crystal structure of Porphyromonas gingivalis SOD===
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Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site.,Yamakura F, Sugio S, Hiraoka BY, Ohmori D, Yokota T Biochemistry. 2003 Sep 16;42(36):10790-9. PMID:12962504<ref>PMID:12962504</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1uer" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12962504}}, adds the Publication Abstract to the page
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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12962504 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12962504}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1UER is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UER OCA].
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==Reference==
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<ref group="xtra">PMID:12962504</ref><ref group="xtra">PMID:10848964</ref><references group="xtra"/>
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[[Category: Porphyromonas gingivalis]]
[[Category: Porphyromonas gingivalis]]
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[[Category: Superoxide dismutase]]
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[[Category: Hiraoka BY]]
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[[Category: Hiraoka, B Y.]]
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[[Category: Ohmori D]]
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[[Category: Ohmori, D.]]
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[[Category: Sugio S]]
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[[Category: Sugio, S.]]
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[[Category: Yamakura F]]
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[[Category: Yamakura, F.]]
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[[Category: Yokota T]]
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[[Category: Yokota, T.]]
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[[Category: Cambialistic]]
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[[Category: Metal-specific]]
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[[Category: Sod]]
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[[Category: Superoxide dismutase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:11:27 2009''
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Current revision

Crystal structure of Porphyromonas gingivalis SOD

PDB ID 1uer

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