3m2e
From Proteopedia
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| - | [[ | + | ==Crystallographic and Single Crystal Spectral Analysis of the Peroxidase Ferryl Intermediate== | 
| + | <StructureSection load='3m2e' size='340' side='right' caption='[[3m2e]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3m2e]] is a 1 chain structure with 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=3M2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M2E FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dso|1dso]], [[2v23|2v23]], [[1dsg|1dsg]], [[1zby|1zby]], [[5ccp|5ccp]], [[3e2n|3e2n]], [[3e2o|3e2o]], [[3m23|3m23]], [[3m25|3m25]], [[3m26|3m26]], [[3m27|3m27]], [[3m28|3m28]], [[3m29|3m29]], [[3m2a|3m2a]], [[3m2b|3m2b]], [[3m2c|3m2c]], [[3m2d|3m2d]], [[3m2f|3m2f]], [[3m2g|3m2g]], [[3m2h|3m2h]], [[3m2i|3m2i]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCP, CCP1, CPO, YKR066C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m2e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m2e RCSB], [http://www.ebi.ac.uk/pdbsum/3m2e PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + |   <jmolCheckbox> | ||
| + |     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m2/3m2e_consurf.spt"</scriptWhenChecked> | ||
| + |     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + |     <text>to colour the structure by Evolutionary Conservation</text> | ||
| + |   </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ferryl [Fe(IV)O] intermediate is important in many heme enzymes, and thus, the precise nature of the Fe(IV)-O bond is critical in understanding enzymatic mechanisms. The 1.40 A crystal structure of cytochrome c peroxidase Compound I has been determined as a function of X-ray dose while the visible spectrum was being monitored. The Fe-O bond increases in length from 1.73 A in the low-X-ray dose structure to 1.90 A in the high-dose structure. The low-dose structure correlates well with an Fe(IV) horizontal lineO bond, while we postulate that the high-dose structure is the cryo-trapped Fe(III)-OH species previously thought to be an Fe(IV)-OH species. | ||
| - | + | Crystallographic and single-crystal spectral analysis of the peroxidase ferryl intermediate.,Meharenna YT, Doukov T, Li H, Soltis SM, Poulos TL Biochemistry. 2010 Apr 13;49(14):2984-6. PMID:20230048<ref>PMID:20230048</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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| ==See Also== | ==See Also== | ||
| *[[Cytochrome c peroxidase|Cytochrome c peroxidase]] | *[[Cytochrome c peroxidase|Cytochrome c peroxidase]] | ||
| - | + | == References == | |
| - | == | + | <references/> | 
| - | < | + | __TOC__ | 
| + | </StructureSection> | ||
| [[Category: Cytochrome-c peroxidase]] | [[Category: Cytochrome-c peroxidase]] | ||
| [[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Meharenna, Y T | + | [[Category: Meharenna, Y T]] | 
| - | [[Category: Poulos, T L | + | [[Category: Poulos, T L]] | 
| [[Category: Heme]] | [[Category: Heme]] | ||
| [[Category: Hydrogen peroxide]] | [[Category: Hydrogen peroxide]] | ||
Revision as of 09:01, 9 December 2014
Crystallographic and Single Crystal Spectral Analysis of the Peroxidase Ferryl Intermediate
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