2d6c

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[[Image:2d6c.gif|left|200px]]
 
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==Crystal structure of myoglobin reconstituted with iron porphycene==
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The line below this paragraph, containing "STRUCTURE_2d6c", creates the "Structure Box" on the page.
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<StructureSection load='2d6c' size='340' side='right'caption='[[2d6c]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2d6c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D6C FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.26&#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=HME:PORPHYCENE+CONTAINING+FE'>HME</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
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{{STRUCTURE_2d6c| PDB=2d6c | SCENE= }}
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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=2d6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d6c OCA], [https://pdbe.org/2d6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d6c RCSB], [https://www.ebi.ac.uk/pdbsum/2d6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d6c ProSAT], [https://www.topsan.org/Proteins/RSGI/2d6c TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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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/d6/2d6c_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=2d6c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The incorporation of an artificially created metal complex into an apomyoglobin is one of the attractive methods in a series of hemoprotein modifications. Single crystals of sperm whale myoglobin reconstituted with 13,16-dicarboxyethyl-2,7-diethyl-3,6,12,17-tetramethylporphycenatoiron(III ) were obtained in the imidazole buffer, and the 3D structure with a 2.25-A resolution indicates that the iron porphycene, a structural isomer of hemin, is located in the normal position of the heme pocket. Furthermore, it was found that the reconstituted myoglobin catalyzed the H2O2-dependent oxidations of substrates such as guaiacol, thioanisole, and styrene. At pH 7.0 and 20 degrees C, the initial rate of the guaiacol oxidation is 11-fold faster than that observed for the native myoglobin. Moreover, the stopped-flow analysis of the reaction of the reconstituted protein with H2O2 suggested the formation of two reaction intermediates, compounds II- and III-like species, in the absence of a substrate. It is a rare example that compound III is formed via compound II in myoglobin chemistry. The enhancement of the peroxidase activity and the formation of the stable compound III in myoglobin with iron porphycene mainly arise from the strong coordination of the Fe-His93 bond.
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'''Crystal structure of myoglobin reconstituted with iron porphycene'''
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Crystal structure and peroxidase activity of myoglobin reconstituted with iron porphycene.,Hayashi T, Murata D, Makino M, Sugimoto H, Matsuo T, Sato H, Shiro Y, Hisaeda Y Inorg Chem. 2006 Dec 25;45(26):10530-6. PMID:17173408<ref>PMID:17173408</ref>
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==Overview==
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The incorporation of an artificially created metal complex into an apomyoglobin is one of the attractive methods in a series of hemoprotein modifications. Single crystals of sperm whale myoglobin reconstituted with 13,16-dicarboxyethyl-2,7-diethyl-3,6,12,17-tetramethylporphycenatoiron(III ) were obtained in the imidazole buffer, and the 3D structure with a 2.25-A resolution indicates that the iron porphycene, a structural isomer of hemin, is located in the normal position of the heme pocket. Furthermore, it was found that the reconstituted myoglobin catalyzed the H2O2-dependent oxidations of substrates such as guaiacol, thioanisole, and styrene. At pH 7.0 and 20 degrees C, the initial rate of the guaiacol oxidation is 11-fold faster than that observed for the native myoglobin. Moreover, the stopped-flow analysis of the reaction of the reconstituted protein with H2O2 suggested the formation of two reaction intermediates, compounds II- and III-like species, in the absence of a substrate. It is a rare example that compound III is formed via compound II in myoglobin chemistry. The enhancement of the peroxidase activity and the formation of the stable compound III in myoglobin with iron porphycene mainly arise from the strong coordination of the Fe-His93 bond.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2D6C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D6C OCA].
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</div>
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<div class="pdbe-citations 2d6c" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Crystal structure and peroxidase activity of myoglobin reconstituted with iron porphycene., Hayashi T, Murata D, Makino M, Sugimoto H, Matsuo T, Sato H, Shiro Y, Hisaeda Y, Inorg Chem. 2006 Dec 25;45(26):10530-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17173408 17173408]
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*[[Myoglobin 3D structures|Myoglobin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
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[[Category: Single protein]]
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[[Category: Hayashi T]]
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[[Category: Hayashi, T.]]
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[[Category: Hisaeda Y]]
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[[Category: Hisaeda, Y.]]
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[[Category: Makino M]]
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[[Category: Makino, M.]]
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[[Category: Matsuo T]]
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[[Category: Matsuo, T.]]
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[[Category: Murata D]]
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[[Category: Murata, D.]]
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[[Category: Sato H]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Shiro Y]]
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[[Category: Sato, H.]]
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[[Category: Sugimoto H]]
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[[Category: Shiro, Y.]]
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[[Category: Sugimoto, H.]]
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[[Category: Hemoprotein]]
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[[Category: Myoglobin]]
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[[Category: Oxygen storage/transport]]
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[[Category: Porphycene]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: Rsgi]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:46:50 2008''
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Current revision

Crystal structure of myoglobin reconstituted with iron porphycene

PDB ID 2d6c

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