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3m38

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Revision as of 05:35, 6 October 2021

The roles of Glutamates and Metal ions in a rationally designed nitric oxide reductase based on myoglobin: I107E FeBMb (No metal ion binding to FeB site)

Structural highlights

3m38 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:
Related:	3m39, 3m3a, 3m3b
Gene:	MB (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 structural and functional model of bacterial nitric oxide reductase (NOR) has been designed by introducing two glutamates (Glu) and three histidines (His) in sperm whale myoglobin. X-ray structural data indicate that the three His and one Glu (V68E) residues bind iron, mimicking the putative Fe(B) site in NOR, while the second Glu (I107E) interacts with a water molecule and forms a hydrogen bonding network in the designed protein. Unlike the first Glu (V68E), which lowered the heme reduction potential by approximately 110 mV, the second Glu has little effect on the heme potential, suggesting that the negatively charged Glu has a different role in redox tuning. More importantly, introducing the second Glu resulted in a approximately 100% increase in NOR activity, suggesting the importance of a hydrogen bonding network in facilitating proton delivery during NOR reactivity. In addition, EPR and X-ray structural studies indicate that the designed protein binds iron, copper, or zinc in the Fe(B) site, each with different effects on the structures and NOR activities, suggesting that both redox activity and an intermediate five-coordinate heme-NO species are important for high NOR activity. The designed protein offers an excellent model for NOR and demonstrates the power of using designed proteins as a simpler and more well-defined system to address important chemical and biological issues.

Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin.,Lin YW, Yeung N, Gao YG, Miner KD, Tian S, Robinson H, Lu Y Proc Natl Acad Sci U S A. 2010 Apr 26. PMID:20421510^[1]

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

References

↑ Lin YW, Yeung N, Gao YG, Miner KD, Tian S, Robinson H, Lu Y. Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin. Proc Natl Acad Sci U S A. 2010 Apr 26. PMID:20421510

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/3m38"

@@ Line 1: / Line 1: @@
 ==The roles of Glutamates and Metal ions in a rationally designed nitric oxide reductase based on myoglobin: I107E FeBMb (No metal ion binding to FeB site)==
-<StructureSection load='3m38' size='340' side='right' caption='[[3m38]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
+<StructureSection load='3m38' size='340' side='right'caption='[[3m38]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3m38]] 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=3M38 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M38 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3m38]] 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=3M38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M38 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m39|3m39]], [[3m3a|3m3a]], [[3m3b|3m3b]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3m39|3m39]], [[3m3a|3m3a]], [[3m3b|3m3b]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([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 ([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=3m38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m38 OCA], [http://pdbe.org/3m38 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m38 RCSB], [http://www.ebi.ac.uk/pdbsum/3m38 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m38 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=3m38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m38 OCA], [https://pdbe.org/3m38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m38 RCSB], [https://www.ebi.ac.uk/pdbsum/3m38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m38 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 32: / Line 32: @@
 ==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: Lin, Y W]]

3m38

From Proteopedia

Revision as of 05:35, 6 October 2021

The roles of Glutamates and Metal ions in a rationally designed nitric oxide reductase based on myoglobin: I107E FeBMb (No metal ion binding to FeB site)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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