1ccg

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(New page: 200px<br /><applet load="1ccg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ccg, resolution 2.1&Aring;" /> '''CONSTRUCTION OF A BIS...)
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[[Image:1ccg.jpg|left|200px]]<br /><applet load="1ccg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ccg, resolution 2.1&Aring;" />
 
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'''CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND'''<br />
 
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==Overview==
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==CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND==
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The crystal structure of the His-175--&gt;Gly (H175G) mutant of cytochrome-c, peroxidase (EC 1.11.1.5), missing its only heme ligand, reveals that the, histidine is replaced by solvent to give a bisaquo heme protein. This, protein retains some residual activity, which can be stimulated or, inhibited by addition of exogenous ligands. Structural analysis confirms, the binding of imidazole to the heme at the position of the wild-type, histidine ligand. This imidazole complex reacts readily with hydrogen, peroxide to produce a radical species with novel properties. However, reactivation in this complex is incomplete (approximately 5%), which, in, view of the very similar structures of the wild-type and the, H175G/imidazole forms, implies a critical role for tethering of the axial, ligand in catalysis. This study demonstrates the feasibility of, constructing heme enzymes with no covalent link to the protein and with, unnatural ligand replacements. Such enzymes may prove useful in studies of, electron transfer mechanisms and in the engineering of novel heme-based, catalysts.
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<StructureSection load='1ccg' size='340' side='right'caption='[[1ccg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ccg]] 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=1CCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CCG 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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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=1ccg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccg OCA], [https://pdbe.org/1ccg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ccg RCSB], [https://www.ebi.ac.uk/pdbsum/1ccg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ccg 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/1ccg_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=1ccg 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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1CCG 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 and IMD 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=1CCG 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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Construction of a bisaquo heme enzyme and binding by exogenous ligands., McRee DE, Jensen GM, Fitzgerald MM, Siegel HA, Goodin DB, Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12847-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7809133 7809133]
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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: Fitzgerald MM]]
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[[Category: Fitzgerald, M.M.]]
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[[Category: Goodin DB]]
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[[Category: Goodin, D.B.]]
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[[Category: Jensen GM]]
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[[Category: Jensen, G.M.]]
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[[Category: Mcree DE]]
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[[Category: Mcree, D.E.]]
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[[Category: Siegel HA]]
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[[Category: Siegel, H.A.]]
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[[Category: HEM]]
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[[Category: IMD]]
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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 12:20:50 2007''
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Current revision

CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND

PDB ID 1ccg

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