View source for 6b6v


==Crystal structure of Desulfovibrio vulgaris carbon monoxide dehydrogenase, as-isolated (protein batch 1), canonical C-cluster==
<StructureSection load='6b6v' size='340' side='right'caption='[[6b6v]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6b6v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B6V 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=6b6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b6v OCA], [https://pdbe.org/6b6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b6v RCSB], [https://www.ebi.ac.uk/pdbsum/6b6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b6v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q72A99_NITV2 Q72A99_NITV2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The C-cluster of the enzyme carbon monoxide dehydrogenase (CODH) is a structurally distinctive Ni-Fe-S cluster employed to catalyze the reduction of CO2 to CO as part of the Wood-Ljungdahl carbon fixation pathway. Using X-ray crystallography, we have observed unprecedented conformational dynamics in the C-cluster of the CODH from Desulfovibrio vulgaris, providing the first view of an oxidized state of the cluster. Combined with supporting spectroscopic data, our structures reveal that this novel, oxidized cluster arrangement plays a role in avoiding irreversible oxidative degradation at the C-cluster. Furthermore, mutagenesis of a conserved cysteine residue that binds the C-cluster in the oxidized state but not in the reduced state suggests that the oxidized conformation could be important for proper cluster assembly, in particular Ni incorporation. Together, these results lay a foundation for future investigations of C-cluster activation and assembly, and contribute to an emerging paradigm of metallocluster plasticity.

Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase.,Wittenborn EC, Merrouch M, Ueda C, Fradale L, Leger C, Fourmond V, Pandelia ME, Dementin S, Drennan CL Elife. 2018 Oct 2;7. pii: 39451. doi: 10.7554/eLife.39451. PMID:30277213<ref>PMID:30277213</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6b6v" style="background-color:#fffaf0;"></div>

==See Also==
*[[Carbon monoxide dehydrogenase 3D structures|Carbon monoxide dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Desulfovibrio vulgaris]]
[[Category: Large Structures]]
[[Category: Drennan CL]]
[[Category: Wittenborn EC]]