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1mkq

From Proteopedia

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[[Image:1mkq.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of the Mutant Variant of Cytochrome c Peroxidase in the 'Open' Uncross-linked form==
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|PDB= 1mkq |SIZE=350|CAPTION= <scene name='initialview01'>1mkq</scene>, resolution 1.64&Aring;
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<StructureSection load='1mkq' size='340' side='right'caption='[[1mkq]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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<table><tr><td colspan='2'>[[1mkq]] 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=1MKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MKQ FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 1.64&#8491;</td></tr>
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|GENE= OPBYC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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}}
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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=1mkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkq OCA], [https://pdbe.org/1mkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mkq RCSB], [https://www.ebi.ac.uk/pdbsum/1mkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mkq 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/mk/1mkq_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=1mkq ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of the Mutant Variant of Cytochrome c Peroxidase in the 'Open' Uncross-linked form'''
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==See Also==
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structure of a cytochrome c peroxidase mutant where the distal catalytic His52 is converted to Tyr reveals that the tyrosine side-chain forms a covalent bond with the indole ring nitrogen atom of Trp51. We hypothesize that this novel bond results from peroxide activation by the heme iron followed by oxidation of Trp51 and Tyr52. This hypothesis has been tested by incorporation of a redox-inactive Zn-protoporphyrin into the protein, and the resulting crystal structure shows the absence of a Trp51-Tyr52 cross-link. Instead, the Tyr52 side-chain orients away from the heme active-site pocket, which requires a substantial rearrangement of residues 72-80 and 134-144. Additional experiments where heme-containing crystals of the mutant were treated with peroxide support our hypothesis that this novel Trp-Tyr cross-link is a peroxide-dependent process mediated by the heme iron.
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[[Category: Large Structures]]
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==About this Structure==
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1MKQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKQ OCA].
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==Reference==
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A novel heme and peroxide-dependent tryptophan-tyrosine cross-link in a mutant of cytochrome c peroxidase., Bhaskar B, Immoos CE, Shimizu H, Sulc F, Farmer PJ, Poulos TL, J Mol Biol. 2003 Apr 18;328(1):157-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12684005 12684005]
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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: Bhaskar B]]
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[[Category: Bhaskar, B.]]
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[[Category: Farmer PJ]]
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[[Category: Farmer, P J.]]
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[[Category: Immoos CE]]
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[[Category: Immoos, C E.]]
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[[Category: Poulos TL]]
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[[Category: Poulos, T L.]]
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[[Category: Shimizu H]]
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[[Category: Shimizu, H.]]
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[[Category: HEM]]
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[[Category: MPD]]
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[[Category: crystal structure]]
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[[Category: cytochrome c peroxidase]]
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[[Category: oxygen radical]]
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[[Category: trp cation radical]]
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[[Category: tryptophan-tyrosine cross-link]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:44:38 2008''
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Current revision

Crystal Structure of the Mutant Variant of Cytochrome c Peroxidase in the 'Open' Uncross-linked form

PDB ID 1mkq

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