3nvr: Difference between revisions

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 ==Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion==
-<StructureSection load='3nvr' size='340' side='right' caption='[[3nvr]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
+<StructureSection load='3nvr' size='340' side='right'caption='[[3nvr]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3nvr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_1.2430 As 1.2430]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NVR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NVR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3nvr]] 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=3NVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NVR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.148&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u55|1u55]], [[3nvu|3nvu]]</td></tr>
+<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tar4, TTE0680 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119072 AS 1.2430])</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=3nvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nvr OCA], [https://pdbe.org/3nvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nvr RCSB], [https://www.ebi.ac.uk/pdbsum/3nvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nvr ProSAT]</span></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=3nvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nvr OCA], [http://pdbe.org/3nvr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nvr RCSB], [http://www.ebi.ac.uk/pdbsum/3nvr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nvr ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 20: @@
 </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=3nvr ConSurf].
 <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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3nvr" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Chemotaxis protein|Chemotaxis protein]]
+*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
 *[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: As 1 2430]]
+[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]]
-[[Category: Kuriyan, J]]
+[[Category: Large Structures]]
-[[Category: Marletta, M A]]
+[[Category: Kuriyan J]]
-[[Category: Olea, C]]
+[[Category: Marletta MA]]
-[[Category: H-nox]]
+[[Category: Olea Jr C]]
-[[Category: Heme cofactor]]
-[[Category: Hemoprotein]]
-[[Category: Signaling protein]]