1dcc

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(New page: 200px<br /><applet load="1dcc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dcc, resolution 2.2&Aring;" /> '''2.2 ANGSTROM STRUCTUR...)
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[[Image:1dcc.gif|left|200px]]<br /><applet load="1dcc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dcc, resolution 2.2&Aring;" />
 
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'''2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX'''<br />
 
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==Overview==
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==2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX==
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The Fe+3-OOH complex of peroxidases has a very short half life, and its, structure cannot be determined by conventional methods. The Fe+2-O2, complex provides a useful structural model for this intermediate, as it, differs by only one electron and one proton from the transient Fe+3-OOH, complex. We therefore determined the crystal structure of the Fe+2-O2, complex formed by a yeast cytochrome c peroxidase mutant with Trp 191, replaced by Phe. The refined structure shows that dioxygen can form a, hydrogen bond with the conserved distal His residue, but not with the, conserved distal Arg residue. When the transient Fe+3-OOH complex is, modelled in a similar orientation, the active site of peroxidase appears, to be optimized for catalysing proton transfer between the vicinal oxygen, atoms of the peroxy-anion.
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<StructureSection load='1dcc' size='340' side='right'caption='[[1dcc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dcc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCC 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]] 2.2&#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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=1dcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcc OCA], [https://pdbe.org/1dcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcc RCSB], [https://www.ebi.ac.uk/pdbsum/1dcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] 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/dc/1dcc_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=1dcc 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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1DCC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with OXY and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DCC OCA].
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*[[Cytochrome c peroxidase|Cytochrome c peroxidase]]
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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==Reference==
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*[[Hemeproteins|Hemeproteins]]
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2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex., Miller MA, Shaw A, Kraut J, Nat Struct Biol. 1994 Aug;1(8):524-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7664080 7664080]
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__TOC__
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[[Category: Cytochrome-c peroxidase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Kraut J]]
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[[Category: Kraut, J.]]
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[[Category: Miller MA]]
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[[Category: Miller, M.A.]]
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[[Category: Shaw A]]
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[[Category: Shaw, A.]]
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[[Category: HEM]]
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[[Category: OXY]]
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[[Category: oxidoreductase(h2o2(a))]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:09:56 2007''
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2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX

PDB ID 1dcc

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