1ccc

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(New page: 200px<br /><applet load="1ccc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ccc, resolution 2.0&Aring;" /> '''THE ASP-HIS-FE TRIAD ...)
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[[Image:1ccc.gif|left|200px]]<br /><applet load="1ccc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ccc, resolution 2.0&Aring;" />
 
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'''THE ASP-HIS-FE TRIAD OF CYTOCHROME C PEROXIDASE CONTROLS THE REDUCTION POTENTIAL, ELECTRONIC STRUCTURE, AND COUPLING OF THE TRYPTOPHAN FREE-RADICAL TO THE HEME'''<br />
 
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==Overview==
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==THE ASP-HIS-FE TRIAD OF CYTOCHROME C PEROXIDASE CONTROLS THE REDUCTION POTENTIAL, ELECTRONIC STRUCTURE, AND COUPLING OF THE TRYPTOPHAN FREE-RADICAL TO THE HEME==
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The buried charge of Asp-235 in cytochrome c peroxidase (CCP) forms an, important hydrogen bond to the histidine ligand of the heme iron. The, Asp-His-metal interaction, which is similar to the catalytic triad of, serine proteases, is found at the active site of many metalloenzymes and, is believed to modulate the character of histidine as a metal ligand. We, have examined the influence of this interaction in CCP on the function, redox properties, and iron zero-field splitting in the native ferric state, and its effect on the Trp-191 free radical site in the oxidized ES, complex. Unlike D235A and D235N, the mutation D235E introduces very little, perturbation in the X-ray crystal structure of the enzyme active site, with only minor changes in the geometry of the carboxylate-histidine, interaction and no observable change at the Trp-191 free radical site., More significant effects are observed in the position of the helix, containing residue Glu-235. However, the small change in hydrogen bond, geometry is all that is necessary to (1) increase the reduction potential, by 70 mV, (2) alter the anisotropy of the Trp-191 free radical EPR, (3), affect the activity and spin-state equilibrium, and (4) reduce the, strength of the iron ligand field as measured by the zero-field splitting., The changes in the redox potential with substitution are correlated with, the observed zero-field splitting, suggesting that redox control is, exerted through the heme ligand by a combination of electrostatic and, ligand field effects. The replacement of Asp-235 with Glu appears to, result in a significantly weaker hydrogen bond in which the proton resides, essentially with His-175. This hydrogen bond is nevertheless strong enough, to prevent the reorientation of Trp-191 and the conversion to one of two, low-spin states observed for D235A and D235N. The Asp-His-Fe interaction, is therefore as important in defining the redox properties and imidazolate, character of His-175 as has been proposed, yet its most important role in, peroxidase function may be to correctly orient Trp-191 for efficient, coupling of the free radical to the heme and to maintain a high-spin, 5-coordinate heme center.
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<StructureSection load='1ccc' size='340' side='right'caption='[[1ccc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ccc]] 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=1CCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CCC 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&#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></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=1ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccc OCA], [https://pdbe.org/1ccc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ccc RCSB], [https://www.ebi.ac.uk/pdbsum/1ccc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ccc 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/cc/1ccc_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=1ccc 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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1CCC 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 HEM as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1CCC OCA].
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme., Goodin DB, McRee DE, Biochemistry. 1993 Apr 6;32(13):3313-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8384877 8384877]
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[[Category: Large Structures]]
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[[Category: Cytochrome-c peroxidase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Goodin DB]]
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[[Category: Goodin, D.B.]]
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[[Category: Mcree DE]]
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[[Category: Mcree, D.E.]]
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[[Category: HEM]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:20:33 2007''
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Current revision

THE ASP-HIS-FE TRIAD OF CYTOCHROME C PEROXIDASE CONTROLS THE REDUCTION POTENTIAL, ELECTRONIC STRUCTURE, AND COUPLING OF THE TRYPTOPHAN FREE-RADICAL TO THE HEME

PDB ID 1ccc

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