2b7s: Difference between revisions

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OCA

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 ==R381K mutant of flavocytochrome c3==
-<StructureSection load='2b7s' size='340' side='right' caption='[[2b7s]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
+<StructureSection load='2b7s' size='340' side='right'caption='[[2b7s]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2b7s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acam_591 Acam 591]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B7S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2b7s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_frigidimarina Shewanella frigidimarina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B7S FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.12&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qjd|1qjd]], [[2b7r|2b7r]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56812 ACAM 591])</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=2b7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b7s OCA], [https://pdbe.org/2b7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b7s RCSB], [https://www.ebi.ac.uk/pdbsum/2b7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b7s ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </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=2b7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b7s OCA], [http://pdbe.org/2b7s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b7s RCSB], [http://www.ebi.ac.uk/pdbsum/2b7s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b7s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FRDA_SHEFR FRDA_SHEFR]] Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional.
+[https://www.uniprot.org/uniprot/FCCA_SHEFR FCCA_SHEFR] Flavocytochrome that catalyzes the reduction of fumarate to succinate (PubMed:10978153). Is essential for fumarate respiration during anaerobic growth, acting as the terminal reductase (By similarity). Receives electrons from the membrane-bound tetraheme c-type cytochrome CymA (By similarity). In vitro, can use the artificial electron donor methyl viologen (PubMed:10978153).[UniProtKB:P83223][UniProtKB:Q07WU7]<ref>PMID:10978153</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b7/2b7s_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 33: / Line 31: @@
 ==See Also==
-*[[Flavocytochrome|Flavocytochrome]]
+*[[Flavocytochrome 3D structures|Flavocytochrome 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Acam 591]]
+[[Category: Large Structures]]
-[[Category: Succinate dehydrogenase]]
+[[Category: Shewanella frigidimarina]]
-[[Category: Chapman, S K]]
+[[Category: Chapman SK]]
-[[Category: Miles, C S]]
+[[Category: Miles CS]]
-[[Category: Mowat, C G]]
+[[Category: Mowat CG]]
-[[Category: Pankhurst, K L]]
+[[Category: Pankhurst KL]]
-[[Category: Reid, G A]]
+[[Category: Reid GA]]
-[[Category: Rothery, E L]]
+[[Category: Rothery EL]]
-[[Category: Walkinshaw, M D]]
+[[Category: Walkinshaw MD]]
-[[Category: Flavocytochrome c3]]
-[[Category: Fumarate reductase]]
-[[Category: Oxidoreductase]]
-[[Category: Proton delivery]]