2bs3: Difference between revisions

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-{{Seed}}
-[[Image:2bs3.png|left|200px]]
-<!--
+==GLU C180 -> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES==
-The line below this paragraph, containing "STRUCTURE_2bs3", creates the "Structure Box" on the page.
+<StructureSection load='2bs3' size='340' side='right'caption='[[2bs3]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2bs3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BS3 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-{{STRUCTURE_2bs3|  PDB=2bs3  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bs3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bs3 OCA], [https://pdbe.org/2bs3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bs3 RCSB], [https://www.ebi.ac.uk/pdbsum/2bs3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bs3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FRDA_WOLSU FRDA_WOLSU] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor.
+== 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/bs/2bs3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2bs3 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Reconciliation of apparently contradictory experimental results obtained on the quinol:fumarate reductase, a diheme-containing respiratory membrane protein complex from Wolinella succinogenes, was previously obtained by the proposal of the so-called "E pathway hypothesis." According to this hypothesis, transmembrane electron transfer via the heme groups is strictly coupled to cotransfer of protons via a transiently established pathway thought to contain the side chain of residue Glu-C180 as the most prominent component. Here we demonstrate that, after replacement of Glu-C180 with Gln or Ile by site-directed mutagenesis, the resulting mutants are unable to grow on fumarate, and the membrane-bound variant enzymes lack quinol oxidation activity. Upon solubilization, however, the purified enzymes display approximately 1/10 of the specific quinol oxidation activity of the wild-type enzyme and unchanged quinol Michaelis constants, K(m). The refined x-ray crystal structures at 2.19 A and 2.76 A resolution, respectively, rule out major structural changes to account for these experimental observations. Changes in the oxidation-reduction heme midpoint potential allow the conclusion that deprotonation of Glu-C180 in the wild-type enzyme facilitates the reoxidation of the reduced high-potential heme. Comparison of solvent isotope effects indicates that a rate-limiting proton transfer step in the wild-type enzyme is lost in the Glu-C180 --&gt; Gln variant. The results provide experimental evidence for the validity of the E pathway hypothesis and for a crucial functional role of Glu-C180.
-===GLU C180-> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES===
+Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase.,Lancaster CR, Sauer US, Gross R, Haas AH, Graf J, Schwalbe H, Mantele W, Simon J, Madej MG Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18860-5. PMID:16380425<ref>PMID:16380425</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16380425}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2bs3" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16380425 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16380425}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-BS3 is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BS3 OCA].
-==Reference==
-<ref group="xtra">PMID:16380425</ref><references group="xtra"/>
-[[Category: Succinate dehydrogenase]]
 [[Category: Wolinella succinogenes]]
-[[Category: Lancaster, C R.D.]]
+[[Category: Lancaster CRD]]
-[[Category: 2fe-2]]
-[[Category: 3d-structure]]
-[[Category: 3fe-4]]
-[[Category: 4fe-4]]
-[[Category: Citric acid cycle]]
-[[Category: Dihaem cytochrome b]]
-[[Category: Electron transport]]
-[[Category: Fad]]
-[[Category: Flavoprotein]]
-[[Category: Fumarate reductase]]
-[[Category: Heme]]
-[[Category: Ion-sulphur protein]]
-[[Category: Iron]]
-[[Category: Iron-sulfur]]
-[[Category: Metal-binding]]
-[[Category: Oxidoreductase]]
-[[Category: Respiratory chain]]
-[[Category: Succinate dehydrogenase]]
-[[Category: Transmembrane]]
-[[Category: Tricarboxylic acid cycle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:13:57 2009''