2d6c: Difference between revisions

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[[Image:2d6c.png|left|200px]]
==Crystal structure of myoglobin reconstituted with iron porphycene==
<StructureSection load='2d6c' size='340' side='right' caption='[[2d6c]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2d6c]] is a 2 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D6C FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HME:PORPHYCENE+CONTAINING+FE'>HME</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene><br>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d6c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2d6c RCSB], [http://www.ebi.ac.uk/pdbsum/2d6c PDBsum], [http://www.topsan.org/Proteins/RSGI/2d6c TOPSAN]</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/d6/2d6c_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 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.


{{STRUCTURE_2d6c|  PDB=2d6c  |  SCENE=  }}
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>


===Crystal structure of myoglobin reconstituted with iron porphycene===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_17173408}}
 
==About this Structure==
[[2d6c]] is a 2 chain structure with 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].


==See Also==
==See Also==
*[[Myoglobin|Myoglobin]]
*[[Myoglobin|Myoglobin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:017173408</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
[[Category: Hayashi, T.]]
[[Category: Hayashi, T.]]

Revision as of 08:04, 29 September 2014

Crystal structure of myoglobin reconstituted with iron porphyceneCrystal structure of myoglobin reconstituted with iron porphycene

Structural highlights

2d6c is a 2 chain structure with sequence from Physeter catodon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, RCSB, PDBsum, TOPSAN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Hayashi T, Murata D, Makino M, Sugimoto H, Matsuo T, Sato H, Shiro Y, Hisaeda Y. Crystal structure and peroxidase activity of myoglobin reconstituted with iron porphycene. Inorg Chem. 2006 Dec 25;45(26):10530-6. PMID:17173408 doi:10.1021/ic061130x

2d6c, resolution 2.26Å

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