3mn0: Difference between revisions

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{{Seed}}
[[Image:3mn0.jpg|left|200px]]


<!--
==Introducing a 2-His-1-Glu Non-Heme Iron Center into Myoglobin confers Nitric Oxide Reductase activity: Cu(II)-CN-FeBMb(-His) form==
The line below this paragraph, containing "STRUCTURE_3mn0", creates the "Structure Box" on the page.
<StructureSection load='3mn0' size='340' side='right'caption='[[3mn0]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3mn0]] 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=3MN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MN0 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
{{STRUCTURE_3mn0|  PDB=3mn0  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mn0 OCA], [https://pdbe.org/3mn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mn0 RCSB], [https://www.ebi.ac.uk/pdbsum/3mn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mn0 ProSAT]</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/mn/3mn0_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=3mn0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A conserved 2-His-1-Glu metal center, as found in natural nonheme iron-containing enzymes, was engineered into sperm whale myoglobin by replacing Leu29 and Phe43 with Glu and His, respectively (swMb L29E, F43H, H64, called Fe(B)Mb(-His)). A high resolution (1.65 A) crystal structure of Cu(II)-CN(-)-Fe(B)Mb(-His) was determined, demonstrating that the unique 2-His-1-Glu metal center was successfully created within swMb. The Fe(B)Mb(-His) can bind Cu, Fe, or Zn ions, with both Cu(I)-Fe(B)Mb(-His) and Fe(II)-Fe(B)Mb(-His) exhibiting nitric oxide reductase (NOR) activities. Cu dependent NOR activity was significantly higher than that of Fe in the same metal binding site. EPR studies showed that the reduction of NO to N(2)O catalyzed by these two enzymes resulted in different intermediates; a five-coordinate heme-NO species was observed for Cu(I)-Fe(B)Mb(-His) due to the cleavage of the proximal heme Fe-His bond, while Fe(II)-Fe(B)Mb(-His) remained six-coordinate. Therefore, both the metal ligand, Glu29, and the metal itself, Cu or Fe, play crucial roles in NOR activity. This study presents a novel protein model of NOR and provides insights into a newly discovered member of the NOR family, gNOR.


===Introducing a 2-His-1-Glu Non-Heme Iron Center into Myoglobin confers Nitric Oxide Reductase activity: Cu(II)-CN-FeBMb(-His) form===
Introducing a 2-His-1-Glu nonheme iron center into myoglobin confers nitric oxide reductase activity.,Lin YW, Yeung N, Gao YG, Miner KD, Lei L, Robinson H, Lu Y J Am Chem Soc. 2010 Jul 28;132(29):9970-2. PMID:20586490<ref>PMID:20586490</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3mn0" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_20586490}}, adds the Publication Abstract to the page
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 20586490 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_20586490}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3MN0 is a 1 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=3MN0 OCA].
 
==Reference==
<ref group="xtra">PMID:20586490</ref><references group="xtra"/>
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
[[Category: Gao, Y G.]]
[[Category: Gao Y-G]]
[[Category: Lei, L.]]
[[Category: Lei L]]
[[Category: Lin, Y W.]]
[[Category: Lin Y-W]]
[[Category: Lu, Y.]]
[[Category: Lu Y]]
[[Category: Miner, K D.]]
[[Category: Miner KD]]
[[Category: Robinson, H.]]
[[Category: Robinson H]]
[[Category: Yeung, N.]]
[[Category: Yeung N]]
[[Category: Alpha helix]]
[[Category: Cyanide]]
[[Category: Heme]]
[[Category: Metal binding protein]]
[[Category: Metal-binding]]
[[Category: No reductase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 11 23:56:59 2010''

Latest revision as of 09:45, 13 August 2026

Introducing a 2-His-1-Glu Non-Heme Iron Center into Myoglobin confers Nitric Oxide Reductase activity: Cu(II)-CN-FeBMb(-His) form

3mn0, resolution 1.65Å

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