2vm0: Difference between revisions

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[[Image:2vm0.png|left|200px]]


{{STRUCTURE_2vm0| PDB=2vm0 | SCENE= }}
==Crystal structure of radiation-induced myoglobin compound II generated after annealing of peroxymyoglobin==
<StructureSection load='2vm0' size='340' side='right'caption='[[2vm0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vm0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VM0 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</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=2vm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vm0 OCA], [https://pdbe.org/2vm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vm0 RCSB], [https://www.ebi.ac.uk/pdbsum/2vm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vm0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] 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/vm/2vm0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2vm0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Myoglobin has the ability to react with hydrogen peroxide, generating high-valent complexes similar to peroxidases (compounds I and II), and in the presence of excess hydrogen peroxide a third intermediate, compound III, with an oxymyoglobin-type structure is generated from compound II. The compound III is, however, easily one-electron reduced to peroxymyoglobin by synchrotron radiation during crystallographic data collection. We have generated and solved the 1.30 A (1 A=0.1 nm) resolution crystal structure of the peroxymyoglobin intermediate, which is isoelectric to compound 0 and has a Fe-O distance of 1.8 A and O-O bond of 1.3 A in accordance with a Fe(II)-O-O- (or Fe(III)-O-O2-) structure. The generation of the peroxy intermediate through reduction of compound III by X-rays shows the importance of using single-crystal microspectrophotometry when doing crystallography on metalloproteins. After having collected crystallographic data on a peroxy-generated myoglobin crystal, we were able (by a short annealing) to break the O-O bond leading to formation of compound II. These results indicate that the cryoradiolytic-generated peroxymyoglobin is biologically relevant through its conversion into compound II upon heating. Additionally, we have observed that the Xe1 site is occupied by a water molecule, which might be the leaving group in the compound II to compound III reaction.


===CRYSTAL STRUCTURE OF RADIATION-INDUCED MYOGLOBIN COMPOUND II GENERATED AFTER ANNEALING OF PEROXYMYOGLOBIN===
The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection.,Hersleth HP, Hsiao YW, Ryde U, Gorbitz CH, Andersson KK Biochem J. 2008 Jun 1;412(2):257-64. PMID:18215120<ref>PMID:18215120</ref>


{{ABSTRACT_PUBMED_18215120}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2vm0" style="background-color:#fffaf0;"></div>
[[2vm0]] is a 1 chain structure of [[Myoglobin]] with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VM0 OCA].


==See Also==
==See Also==
*[[Myoglobin|Myoglobin]]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:018215120</ref><ref group="xtra">PMID:011935353</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Andersson, K K.]]
[[Category: Large Structures]]
[[Category: Gorbitz, C H.]]
[[Category: Andersson KK]]
[[Category: Hersleth, H P.]]
[[Category: Gorbitz CH]]
[[Category: Ferryl]]
[[Category: Hersleth H-P]]
[[Category: Haem]]
[[Category: Heme]]
[[Category: Iron]]
[[Category: Metal-binding]]
[[Category: Monooxygenase]]
[[Category: Muscle protein]]
[[Category: Oxygen activation]]
[[Category: Oxygen transport]]
[[Category: Peroxidase]]
[[Category: Radiolytic- reduction]]
[[Category: Reaction intermediate]]
[[Category: Transport]]
[[Category: X-ray-induced-photoreduction]]
Retrieved from "https://proteopedia.org/2vm0"