6eno
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Double cubane cluster oxidoreductase== | |
| + | <StructureSection load='6eno' size='340' side='right'caption='[[6eno]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6eno]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans_Z-2901 Carboxydothermus hydrogenoformans Z-2901]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ENO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ENO 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]] 1.635Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BJ8:Double+cubane+cluster'>BJ8</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6eno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eno OCA], [https://pdbe.org/6eno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eno RCSB], [https://www.ebi.ac.uk/pdbsum/6eno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eno ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q3AET9_CARHZ Q3AET9_CARHZ] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Chemically demanding reductive conversions in biology, such as the reduction of dinitrogen to ammonia or the Birch-type reduction of aromatic compounds, depend on Fe/S-cluster-containing ATPases. These reductions are typically catalyzed by two-component systems, in which an Fe/S-cluster-containing ATPase energizes an electron to reduce a metal site on the acceptor protein that drives the reductive reaction. Here, we show a two-component system featuring a double-cubane [Fe8S9]-cluster [{Fe4S4(SCys)3}2(mu2-S)]. The double-cubane-cluster-containing enzyme is capable of reducing small molecules, such as acetylene (C2H2), azide (N3(-)), and hydrazine (N2H4). We thus present a class of metalloenzymes akin in fold, metal clusters, and reactivity to nitrogenases. | ||
| - | + | ATP-dependent substrate reduction at an [Fe8S9] double-cubane cluster.,Jeoung JH, Dobbek H Proc Natl Acad Sci U S A. 2018 Mar 5. pii: 1720489115. doi:, 10.1073/pnas.1720489115. PMID:29507223<ref>PMID:29507223</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Dobbek | + | <div class="pdbe-citations 6eno" style="background-color:#fffaf0;"></div> |
| - | [[Category: Jeoung | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Carboxydothermus hydrogenoformans Z-2901]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dobbek H]] | ||
| + | [[Category: Jeoung JH]] | ||
Current revision
Double cubane cluster oxidoreductase
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