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1bzo

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(New page: 200px<br /><applet load="1bzo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bzo, resolution 2.1&Aring;" /> '''THREE-DIMENSIONAL STR...)
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[[Image:1bzo.jpg|left|200px]]<br /><applet load="1bzo" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bzo, resolution 2.1&Aring;" />
 
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'''THREE-DIMENSIONAL STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE FROM P.LEIOGNATHI, SOLVED BY X-RAY CRYSTALLOGRAPHY.'''<br />
 
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==Overview==
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==THREE-DIMENSIONAL STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE FROM P.LEIOGNATHI, SOLVED BY X-RAY CRYSTALLOGRAPHY.==
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Prokaryotic Cu,Zn superoxide dismutases are characterized by a distinct, quaternary structure, as compared to that of the homologous eukaryotic, enzymes. Here we report a newly determined crystal structure of the, dimeric Cu,Zn superoxide dismutase from Photobacterium leiognathi, (crystallized in space group R32, refined at 2.5 A resolution, R-factor, 0.19) and analyse it in comparison with that of the monomeric enzyme from, Escherichia coli. The dimeric assembly, observed also in a previously, studied monoclinic crystal form of P. leiognathi Cu,Zn superoxide, dismutase, is based on a ring-shaped subunit contact region, defining a, solvated interface cavity. Three clusters of neighbouring residues play a, direct role in the stabilization of the quaternary assembly. The present, analysis, extended to the amino acid sequences of the other 11 known, prokaryotic Cu,Zn superoxide dismutases, shows that at least in five other, prokaryotic enzymes the interface residue clusters are under strong, evolutionary constraint, suggesting the attainment of a quaternary, structure coincident with that of P. leiognathi Cu,Zn superoxide, dismutase. Calculation of electrostatic fields for both the enzymes from, E. coli and P. leiognathi shows that the monomeric/dimeric association, behaviour displayed by prokaryotic Cu, Zn superoxide dismutases is related, to the distribution of surface charged residues. Moreover, Brownian, dynamics simulations reproduce closely the observed enzyme:substrate, association rates, highlighting the role of the active site neighbouring, residues in determining the dismutase catalytic properties.
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<StructureSection load='1bzo' size='340' side='right'caption='[[1bzo]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bzo]] 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=1BZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BZO FirstGlance]. <br>
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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]] 2.1&#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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=1bzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bzo OCA], [https://pdbe.org/1bzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bzo RCSB], [https://www.ebi.ac.uk/pdbsum/1bzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bzo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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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/bz/1bzo_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=1bzo ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1BZO 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, CU and IUM 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BZO OCA].
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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase., Bordo D, Matak D, Djinovic-Carugo K, Rosano C, Pesce A, Bolognesi M, Stroppolo ME, Falconi M, Battistoni A, Desideri A, J Mol Biol. 1999 Jan 8;285(1):283-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9878406 9878406]
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[[Category: Large Structures]]
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[[Category: Photobacterium leiognathi]]
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[[Category: Photobacterium leiognathi subsp. leiognathi]]
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[[Category: Single protein]]
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[[Category: Battistoni A]]
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[[Category: Superoxide dismutase]]
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[[Category: Bolognesi M]]
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[[Category: Battistoni, A.]]
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[[Category: Bordo D]]
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[[Category: Bolognesi, M.]]
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[[Category: Desideri A]]
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[[Category: Bordo, D.]]
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[[Category: Djinovic-Carugo K]]
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[[Category: Desideri, A.]]
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[[Category: Falconi M]]
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[[Category: Djinovic-Carugo, K.]]
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[[Category: Matak D]]
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[[Category: Falconi, M.]]
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[[Category: Pesce A]]
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[[Category: Matak, D.]]
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[[Category: Rosano C]]
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[[Category: Pesce, A.]]
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[[Category: Stroppolo ME]]
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[[Category: Rosano, C.]]
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[[Category: Stroppolo, M.E.]]
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[[Category: CU]]
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[[Category: IUM]]
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[[Category: ZN]]
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[[Category: monomeric cu]]
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[[Category: protein electrostatic]]
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[[Category: protein-subunit recognition]]
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[[Category: zn superoxide dismutase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:02:40 2007''
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Current revision

THREE-DIMENSIONAL STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE FROM P.LEIOGNATHI, SOLVED BY X-RAY CRYSTALLOGRAPHY.

PDB ID 1bzo

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