2ekt: Difference between revisions

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[[Image:2ekt.png|left|200px]]


{{STRUCTURE_2ekt| PDB=2ekt | SCENE= }}
==Crystal structure of myoglobin reconstituted with 6-methyl-6-depropionatehemin==
<StructureSection load='2ekt' size='340' side='right'caption='[[2ekt]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ekt]] is a 1 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=2EKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EKT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6HE:6-METHY-6-DEPROPIONATEHEMIN'>6HE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ekt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ekt OCA], [https://pdbe.org/2ekt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ekt RCSB], [https://www.ebi.ac.uk/pdbsum/2ekt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ekt ProSAT], [https://www.topsan.org/Proteins/RSGI/2ekt TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
== 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/ek/2ekt_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/main_output.php?pdb_ID=2ekt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two heme propionate side chains, which are attached at the 6 and 7 positions of the heme framework, are linked with Arg45 and Ser92, respectively, in sperm whale myoglobin. To evaluate the role of each propionate, two kinds of one-legged hemins, 6-depropionated and 7-depropionated protohemins, were prepared and inserted into the apomyoglobin to yield two reconstituted proteins. Structural data of the reconstituted myoglobins were obtained via an X-ray crystallographic analysis at a resolution of 1.1-1.4 A and resonance Raman spectroscopy. It was found that the lack of the 6-propionate reduces the number of hydrogen bonds in the distal site and clearly changes the position of the Arg45 residue with the disrupting Arg45-Asp60 interaction. In contrast, the removal of the 7-propionate does not cause a significant structural change in the residues of the distal and proximal sites. However, the resonance Raman studies suggested that the coordination bond strength of the His93-Fe bond for the protein with the 7-depropionated protoheme slightly increases compared to that for the protein with the native heme. The O2 and CO ligand binding studies for the reconstituted proteins with the one-legged hemes provide an important insight into the functional role of each propionate. The lack of the 6-propionate accelerates the O2 dissociation by ca. 3-fold compared to those of the other reconstituted and native proteins. The lack of the 7-propionate enhances the CO affinity by 2-fold compared to that of the protein with the native heme. These results indicate that the 6-propionate clearly contributes to the stabilization of the bound O2, whereas the 7-propionate plays an important role in the regulation of the Fe-His bond.


===Crystal structure of myoglobin reconstituted with 6-methyl-6-depropionatehemin===
Structure and ligand binding properties of myoglobins reconstituted with monodepropionated heme: functional role of each heme propionate side chain.,Harada K, Makino M, Sugimoto H, Hirota S, Matsuo T, Shiro Y, Hisaeda Y, Hayashi T Biochemistry. 2007 Aug 21;46(33):9406-16. Epub 2007 Jul 18. PMID:17636874<ref>PMID:17636874</ref>


{{ABSTRACT_PUBMED_17636874}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2ekt" style="background-color:#fffaf0;"></div>
[[2ekt]] is a 1 chain structure of [[Myoglobin]] 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=2EKT OCA].


==See Also==
==See Also==
*[[Myoglobin|Myoglobin]]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:017636874</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
[[Category: Harada, K.]]
[[Category: Harada K]]
[[Category: Hayashi, T.]]
[[Category: Hayashi T]]
[[Category: Hirota, S.]]
[[Category: Hirota S]]
[[Category: Hisaeda, Y.]]
[[Category: Hisaeda Y]]
[[Category: Makino, M.]]
[[Category: Makino M]]
[[Category: Matsuo, T.]]
[[Category: Matsuo T]]
[[Category: Shiro, Y.]]
[[Category: Shiro Y]]
[[Category: Sugimoto, H.]]
[[Category: Sugimoto H]]
[[Category: Globin fold]]
[[Category: Oxygen storage-transport complex]]

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