3nvu
From Proteopedia
(Difference between revisions)
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==Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion== | ==Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion== | ||
| - | <StructureSection load='3nvu' size='340' side='right' caption='[[3nvu]], [[Resolution|resolution]] 2.04Å' scene=''> | + | <StructureSection load='3nvu' size='340' side='right'caption='[[3nvu]], [[Resolution|resolution]] 2.04Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3nvu]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3nvu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NVU FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.038Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=3nvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nvu OCA], [https://pdbe.org/3nvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nvu RCSB], [https://www.ebi.ac.uk/pdbsum/3nvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nvu ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=3nvu ConSurf]. | </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=3nvu ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Hemoproteins are ubiquitous in biology and are commonly involved in critical processes such as electron transfer, oxidative phosphorylation, and signal transduction. Both the protein environment and the heme cofactor contribute to generate the range of chemical properties needed for these diverse functions. Using the heme nitric oxide/oxygen binding (H-NOX) protein from the thermophilic bacterium Thermoanaerobacter tengcongensis, we have shown that heme electronic properties can be modulated by porphyrin distortion within the same protein scaffold without changing the heme ligation state or heme environment. The degree of heme distortion was found to be directly correlated to the electron density at the heme iron, as evidenced by dramatic changes in the heme redox potential and pK(a) of the distal ligand ((-)OH vs H(2)O). Protein-induced porphyrin distortion represents a new strategy to rationally tune the electronic properties of protein-bound porphyrins and could be used to engineer proteins with desired reactivity or functionality. | ||
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| - | Modulating Heme Redox Potential through Protein-Induced Porphyrin Distortion.,Olea C, Kuriyan J, Marletta MA J Am Chem Soc. 2010 Aug 25. PMID:20735135<ref>PMID:20735135</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3nvu" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Chemotaxis protein|Chemotaxis protein]] | + | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] |
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | *[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Kuriyan J]] |
| - | [[Category: | + | [[Category: Marletta MA]] |
| - | [[Category: | + | [[Category: Olea Jr C]] |
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Current revision
Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion
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