3mn0: Difference between revisions
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==Introducing a 2-His-1-Glu Non-Heme Iron Center into Myoglobin confers Nitric Oxide Reductase activity: Cu(II)-CN-FeBMb(-His) form== | |||
<StructureSection load='3mn0' size='340' side='right'caption='[[3mn0]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</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> | |||
<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 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3mn0" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Myoglobin|Myoglobin]] | *[[Myoglobin 3D structures|Myoglobin 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Gao | [[Category: Gao Y-G]] | ||
[[Category: Lei | [[Category: Lei L]] | ||
[[Category: Lin | [[Category: Lin Y-W]] | ||
[[Category: Lu | [[Category: Lu Y]] | ||
[[Category: Miner | [[Category: Miner KD]] | ||
[[Category: Robinson | [[Category: Robinson H]] | ||
[[Category: Yeung | [[Category: Yeung N]] | ||
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
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