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==CryoEM structure of carbon monoxide dehydrogenase from Ruminococcus flavefaciens== | |||
<StructureSection load='28lw' size='340' side='right'caption='[[28lw]], [[Resolution|resolution]] 2.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[28lw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminococcus_flavefaciens Ruminococcus flavefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=28LW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=28LW FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.55Å</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=28lw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=28lw OCA], [https://pdbe.org/28lw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=28lw RCSB], [https://www.ebi.ac.uk/pdbsum/28lw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=28lw ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Carbon monoxide dehydrogenases (CODHs) catalyse the reversible oxidation of CO to CO(2) and play central roles in microbial carbon metabolism. While well-characterised CODHs from different phylogenetic backgrounds exhibit high bidirectional activity, the enigmatic clade B remains functionally uncharacterised. Here, we present the first structural and biochemical characterisation of a clade B CODH from Ruminococcus flavefaciens (RfCODH). It reveals striking divergence from canonical enzymes. A new anaerobic cryo-EM workflow was developed, carried out entirely under anoxic conditions by manual blotting and plunge freezing. It resulted in a 2.53 A RfCODH structure. The structure adopts the typical CODH fold, but exhibits blocked gas channels, a compromised proton transfer pathway and disrupted cofactor coordination. This provides a structural rationale for RfCODH's severely attenuated CO oxidation activity (13 mU/mg vs. 900 U/mg for the well-studied ChCODH-II). EPR spectroscopy reveals unique oxidised C-cluster states not previously characterised in CODHs. Mirror tree analysis hints to co-evolution between clade B CODHs and associated ABC transporter substrate-binding proteins, suggesting these enzymes function in metabolism of substrates imported via the ABC transporter module. All findings indicate evolutionary repurposing of the CODH scaffold for alternative physiological functions. | |||
Beyond Canonical CO Oxidation: Structural and Evolutionary Insights Into a Non-Canonical Carbon Monoxide Dehydrogenase.,Bohm M, Srinivas V, Wiseman B, Huang P, Senger M, Hogbom M, Land H Angew Chem Int Ed Engl. 2026 Sep 21;65(39):e1702233. doi: 10.1002/anie.1702233. , Epub 2026 Jul 24. PMID:42495917<ref>PMID:42495917</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 28lw" style="background-color:#fffaf0;"></div> | ||
[[Category: Hogbom | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ruminococcus flavefaciens]] | |||
[[Category: Hogbom M]] | |||
[[Category: Srinivas V]] | |||
