1oaj: Difference between revisions

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-[[Image:1oaj.jpg|left|200px]]
-<!--
+==Active site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase==
-The line below this paragraph, containing "STRUCTURE_1oaj", creates the "Structure Box" on the page.
+<StructureSection load='1oaj' size='340' side='right'caption='[[1oaj]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1oaj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Photobacterium_leiognathi_subsp._leiognathi Photobacterium leiognathi subsp. leiognathi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAJ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_1oaj|  PDB=1oaj  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oaj OCA], [https://pdbe.org/1oaj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oaj RCSB], [https://www.ebi.ac.uk/pdbsum/1oaj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oaj ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SODC_PHOLE SODC_PHOLE] Destroys 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/oa/1oaj_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=1oaj ConSurf].
+<div style="clear:both"></div>
-'''ACTIVE SITE COPPER AND ZINC IONS MODULATE THE QUATERNARY STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE'''
+==See Also==
+*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The influence of the constitutive metal ions on the equilibrium properties of dimeric Photobacterium leiognathi Cu,Zn superoxide dismutase has been studied for the wild-type and for two mutant protein forms bearing a negative charge in the amino acid clusters at the dimer association interface. Depletion of copper and zinc dissociates the two mutant proteins into monomers, which reassemble toward the dimeric state upon addition of stoichiometric amounts of zinc. Pressure-dependent dissociation is observed for the copper-depleted wild-type and mutated enzymes, as monitored by the fluorescence shift of a unique tryptophan residue located at the subunit association interface. The spectral shift occurs slowly, reaching a plateau after 15-20 minutes, and is fully reversible. The recovery of the original fluorescence properties, after decompression, is fast (less than four minutes), suggesting that the isolated subunit has a relatively stable structure, and excluding the presence of stable intermediates during the dimer-monomer transition. The dimer dissociation process is still incomplete at 6.5 kbar for the copper-depleted wild-type and mutated enzymes, at variance with what is generally observed for oligomeric proteins that dissociate below 3 kbar. Measurement of the degree of dissociation, at two different protein concentrations, allows us to calculate the standard volume variation upon association, Delta V, and the dissociation constant K(d0), at atmospheric pressure, (25 ml/mol and 3 x 10(-7)M, respectively). The holoprotein is fully dimeric even at 6.5 kbar, which allows us to evaluate a lower Delta G degrees limit of 11.5 kcal/mol, corresponding to a dissociation constant K(d0)&lt;10(-9)M.
+[[Category: Large Structures]]
+[[Category: Photobacterium leiognathi subsp. leiognathi]]
-==About this Structure==
+[[Category: Bolognesi M]]
-OAJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Photobacterium_leiognathi Photobacterium leiognathi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAJ OCA].
+[[Category: Castelli S]]
+[[Category: Cioni P]]
-==Reference==
+[[Category: Desideri A]]
-Active-site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase., Cioni P, Pesce A, Morozzo della Rocca B, Castelli S, Falconi M, Parrilli L, Bolognesi M, Strambini G, Desideri A, J Mol Biol. 2003 Mar 7;326(5):1351-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12595249 12595249]
+[[Category: Falconi M]]
-[[Category: Photobacterium leiognathi]]
+[[Category: Parrilli L]]
-[[Category: Single protein]]
+[[Category: Pesce A]]
-[[Category: Superoxide dismutase]]
+[[Category: Rocca BMD]]
-[[Category: Bolognesi, M.]]
+[[Category: Strambini G]]
-[[Category: Castelli, S.]]
-[[Category: Cioni, P.]]
-[[Category: Desideri, A.]]
-[[Category: Falconi, M.]]
-[[Category: Parrilli, L.]]
-[[Category: Pesce, A.]]
-[[Category: Rocca, B M.D.]]
-[[Category: Strambini, G.]]
-[[Category: Oxidoreductase]]
-[[Category: Prokariotic cu]]
-[[Category: Protein electrostatic]]
-[[Category: Subunit interaction recognition]]
-[[Category: Zn superoxide dismutase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:35:47 2008''