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1dj1

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(New page: 200px<br /><applet load="1dj1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dj1, resolution 1.93&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1dj1.gif|left|200px]]<br /><applet load="1dj1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dj1, resolution 1.93&Aring;" />
 
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'''CRYSTAL STRUCTURE OF R48A MUTANT OF CYTOCHROME C PEROXIDASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF R48A MUTANT OF CYTOCHROME C PEROXIDASE==
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Heme enzymes are capable of catalyzing a range of oxidative chemistry with, high specificity, depending on the surrounding protein environment. We, describe here a reaction catalyzed by a mutant of cytochrome c peroxidase, which is similar but distinct from those catalyzed by nitric-oxide, synthase. In the R48A mutant, an expanded water-filled cavity was created, above the distal heme face. N-hydroxyguanidine (NHG) but not guanidine was, shown to bind in the cavity with K(d) = 8.5 mM, and coordinate to the heme, to give a low spin state. Reaction of R48A with peroxide produced a, Fe(IV)=O/Trp(.+) center capable of oxidizing either NHG or, N(omega)-hydroxyarginine (NHA), but not arginine or guanidine, by a, multi-turnover catalytic process. Oxidation of either NHG or NHA by R48A, did not result in the accumulation of NO, NO(2)(-), NO(3)(-), urea, or, citrulline, but instead afforded a yellow product with absorption maxima, of 257 and 400 nm. Mass spectrometry of the derivatized NHA products, identified the yellow species as N-nitrosoarginine. We suggest that a, nitrosylating agent, possibly derived from HNO, is produced by the, oxidation of one molecule of substrate. This then reacts with a second, substrate molecule to form the observed N-nitroso products. This complex, chemistry illustrates how the active sites of enzymes such as nitric-oxide, synthase may serve to prevent alternative reactions from occurring, in, addition to enabling those desired.
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<StructureSection load='1dj1' size='340' side='right'caption='[[1dj1]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dj1]] 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=1DJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DJ1 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]] 1.93&#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=1dj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dj1 OCA], [https://pdbe.org/1dj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dj1 RCSB], [https://www.ebi.ac.uk/pdbsum/1dj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dj1 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/dj/1dj1_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=1dj1 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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1DJ1 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=1DJ1 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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Unusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase., Hirst J, Goodin DB, J Biol Chem. 2000 Mar 24;275(12):8582-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10722697 10722697]
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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: Hirst J]]
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[[Category: Hirst, J.]]
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[[Category: HEM]]
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[[Category: cavity mutant]]
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[[Category: heme enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:19:09 2007''
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Current revision

CRYSTAL STRUCTURE OF R48A MUTANT OF CYTOCHROME C PEROXIDASE

PDB ID 1dj1

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