This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1oaj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:56, 10 April 2024) (edit) (undo)
 
(20 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1oaj.gif|left|200px]]<br />
 
-
<applet load="1oaj" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1oaj, resolution 1.73&Aring;" />
 
-
'''ACTIVE SITE COPPER AND ZINC IONS MODULATE THE QUATERNARY STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE'''<br />
 
-
==Overview==
+
==Active site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase==
-
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.
+
<StructureSection load='1oaj' size='340' side='right'caption='[[1oaj]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
-
==About this Structure==
+
==See Also==
-
1OAJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Photobacterium_leiognathi Photobacterium leiognathi] with ZN and CU as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OAJ OCA].
+
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12595249 12595249]
+
[[Category: Large Structures]]
-
[[Category: Photobacterium leiognathi]]
+
[[Category: Photobacterium leiognathi subsp. leiognathi]]
-
[[Category: Single protein]]
+
[[Category: Bolognesi M]]
-
[[Category: Superoxide dismutase]]
+
[[Category: Castelli S]]
-
[[Category: Bolognesi, M.]]
+
[[Category: Cioni P]]
-
[[Category: Castelli, S.]]
+
[[Category: Desideri A]]
-
[[Category: Cioni, P.]]
+
[[Category: Falconi M]]
-
[[Category: Desideri, A.]]
+
[[Category: Parrilli L]]
-
[[Category: Falconi, M.]]
+
[[Category: Pesce A]]
-
[[Category: Parrilli, L.]]
+
[[Category: Rocca BMD]]
-
[[Category: Pesce, A.]]
+
[[Category: Strambini G]]
-
[[Category: Rocca, B.M.D.]]
+
-
[[Category: Strambini, G.]]
+
-
[[Category: CU]]
+
-
[[Category: ZN]]
+
-
[[Category: oxidoreductase]]
+
-
[[Category: prokariotic cu]]
+
-
[[Category: protein electrostatic]]
+
-
[[Category: subunit interaction recognition]]
+
-
[[Category: zn superoxide dismutase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:19:23 2007''
+

Current revision

Active site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase

PDB ID 1oaj

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oaj"
Personal tools