3m3a: Difference between revisions
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< | ==The roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin: Cu(II)-I107E FeBMb (Cu(II) binding to FeB site)== | ||
<StructureSection load='3m3a' size='340' side='right'caption='[[3m3a]], [[Resolution|resolution]] 1.37Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3m3a]] 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=3M3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M3A 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]] 1.37Å</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=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=3m3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m3a OCA], [https://pdbe.org/3m3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m3a RCSB], [https://www.ebi.ac.uk/pdbsum/3m3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m3a 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/m3/3m3a_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=3m3a ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:20421510</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3m3a" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[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: Lin | [[Category: Lin Y-W]] | ||
[[Category: Lu | [[Category: Lu Y]] | ||
[[Category: Miner | [[Category: Miner KD]] | ||
[[Category: Robinson | [[Category: Robinson H]] | ||
[[Category: Tian | [[Category: Tian S]] | ||
[[Category: Yeung | [[Category: Yeung N]] | ||
Latest revision as of 09:42, 13 August 2026
The roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin: Cu(II)-I107E FeBMb (Cu(II) binding to FeB site)
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