3mn0

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(Difference between revisions)

Revision as of 05:41, 6 October 2021

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

Structural highlights

3mn0 is a 1 chain structure with sequence from Phymc. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	MB, pMbt7-7 (PHYMC)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

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

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^[1]

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

References

↑ Lin YW, Yeung N, Gao YG, Miner KD, Lei L, Robinson H, Lu Y. Introducing a 2-His-1-Glu nonheme iron center into myoglobin confers nitric oxide reductase activity. J Am Chem Soc. 2010 Jul 28;132(29):9970-2. PMID:20586490 doi:10.1021/ja103516n

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3mn0"

@@ Line 1: / Line 1: @@
 ==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]] 1.65&Aring;' scene=''>
+<StructureSection load='3mn0' size='340' side='right'caption='[[3mn0]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mn0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MN0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mn0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phymc Phymc]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB, pMbt7-7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 PHYCD])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB, pMbt7-7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 PHYMC])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mn0 OCA], [http://pdbe.org/3mn0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mn0 RCSB], [http://www.ebi.ac.uk/pdbsum/3mn0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mn0 ProSAT]</span></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 ==
-[[http://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+[[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]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Myoglobin|Myoglobin]]
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Phycd]]
+[[Category: Large Structures]]
+[[Category: Phymc]]
 [[Category: Gao, Y G]]
 [[Category: Lei, L]]

3mn0

From Proteopedia

Revision as of 05:41, 6 October 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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