6elq: Difference between revisions
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New page: '''Unreleased structure''' The entry 6elq is ON HOLD Authors: Domnik, L., Goetzl, S., Jeoung, J.H., Dobbek, H. Description: Carbon Monoxide Dehydrogenase IV from Carboxydothermus hydro... |
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The | ==Carbon Monoxide Dehydrogenase IV from Carboxydothermus hydrogenoformans== | ||
<StructureSection load='6elq' size='340' side='right'caption='[[6elq]], [[Resolution|resolution]] 2.52Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6elq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ELQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ELQ 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]] 2.52Å</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=6elq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6elq OCA], [https://pdbe.org/6elq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6elq RCSB], [https://www.ebi.ac.uk/pdbsum/6elq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6elq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q3AE44_CARHZ Q3AE44_CARHZ] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
CO dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO2 . Genomic analysis indicated that the metabolic functions of CODHs vary. The genome of Carboxydothermus hydrogenoformans encodes five CODHs (CODH-I-V), of which CODH-IV is found in a gene cluster near a peroxide-reducing enzyme. Our kinetic and crystallographic experiments reveal that CODH-IV differs from other CODHs in several characteristic properties: it has a very high affinity for CO, oxidizes CO at diffusion-limited rate over a wide range of temperatures, and is more tolerant to oxygen than CODH-II. Thus, our observations support the idea that CODH-IV is a CO scavenger in defence against oxidative stress and highlight that CODHs are more diverse in terms of reactivity than expected. | |||
CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2.,Domnik L, Merrouch M, Goetzl S, Jeoung JH, Leger C, Dementin S, Fourmond V, Dobbek H Angew Chem Int Ed Engl. 2017 Nov 27;56(48):15466-15469. doi:, 10.1002/anie.201709261. Epub 2017 Nov 2. PMID:29024326<ref>PMID:29024326</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Dobbek | <div class="pdbe-citations 6elq" style="background-color:#fffaf0;"></div> | ||
[[Category: Domnik | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Carbon monoxide dehydrogenase 3D structures|Carbon monoxide dehydrogenase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Carboxydothermus hydrogenoformans]] | |||
[[Category: Large Structures]] | |||
[[Category: Dobbek H]] | |||
[[Category: Domnik L]] | |||
[[Category: Goetzl S]] | |||
[[Category: Jeoung JH]] | |||
Latest revision as of 09:20, 16 September 2026
Carbon Monoxide Dehydrogenase IV from Carboxydothermus hydrogenoformans
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