7b95
From Proteopedia
(Difference between revisions)
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==CooS-V with partially oxidized hybrid cluster by hydroxylamine== | ==CooS-V with partially oxidized hybrid cluster by hydroxylamine== | ||
| - | <StructureSection load='7b95' size='340' side='right'caption='[[7b95]]' scene=''> | + | <StructureSection load='7b95' size='340' side='right'caption='[[7b95]], [[Resolution|resolution]] 1.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B95 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7b95]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B95 FirstGlance]. <br> |
| - | </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=7b95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b95 OCA], [https://pdbe.org/7b95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b95 RCSB], [https://www.ebi.ac.uk/pdbsum/7b95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b95 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SF3:FE4-S3+CLUSTER'>SF3</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Anaerobic_carbon-monoxide_dehydrogenase Anaerobic carbon-monoxide dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.7.4 1.2.7.4] </span></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=7b95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b95 OCA], [https://pdbe.org/7b95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b95 RCSB], [https://www.ebi.ac.uk/pdbsum/7b95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b95 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ni,Fe-containing carbon monoxide dehydrogenases (CODHs) catalyze the reversible reduction of CO2 to CO. Several anaerobic microorganisms encode multiple CODHs in their genome, of which some, despite being annotated as CODHs, lack a cysteine of the canonical binding motif for the active site Ni,Fe-cluster. Here, we report on the structure and reactivity of such a deviant enzyme, termed CooS-VCh . Its structure reveals the typical CODH scaffold, but contains an iron-sulfur-oxo hybrid-cluster. Although closely related to true CODHs, CooS-VCh catalyzes neither CO oxidation, nor CO2 reduction. The active site of CooS-VCh undergoes a redox-dependent restructuring between a reduced [4Fe-3S]-cluster and an oxidized [4Fe-2S-S*-2O-2(H2 O)]-cluster. Hydroxylamine, a slow-turnover substrate of CooS-VCh , oxidizes the hybrid-cluster in two structurally distinct steps. Overall, minor changes in CODHs are sufficient to accommodate a Fe/S/O-cluster in place of the Ni,Fe-heterocubane-cluster of CODHs. | ||
| + | |||
| + | A Morphing [4Fe-3S-nO]-Cluster within a Carbon Monoxide Dehydrogenase Scaffold.,Jeoung JH, Fesseler J, Domnik L, Klemke F, Sinnreich M, Teutloff C, Dobbek H Angew Chem Int Ed Engl. 2022 Apr 25;61(18):e202117000. doi:, 10.1002/anie.202117000. Epub 2022 Mar 4. PMID:35133707<ref>PMID:35133707</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7b95" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Anaerobic carbon-monoxide dehydrogenase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Dobbek H]] | + | [[Category: Dobbek, H]] |
| - | [[Category: Jeoung | + | [[Category: Jeoung, J H]] |
| + | [[Category: Codh]] | ||
| + | [[Category: Hcp]] | ||
| + | [[Category: Hybrid cluster]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 18:10, 27 July 2022
CooS-V with partially oxidized hybrid cluster by hydroxylamine
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