6elq: Difference between revisions
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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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ELQ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BF8:FE(4)-NI(1)-S(5)+CLUSTER+with+Oxygen'>BF8</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anaerobic_carbon-monoxide_dehydrogenase Anaerobic carbon-monoxide dehydrogenase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6elq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6elq OCA], [http://pdbe.org/6elq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6elq RCSB], [http://www.ebi.ac.uk/pdbsum/6elq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6elq ProSAT]</span></td></tr> | |||
</table> | |||
<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> | ||
<div class="pdbe-citations 6elq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Anaerobic carbon-monoxide dehydrogenase]] | |||
[[Category: Dobbek, H]] | [[Category: Dobbek, H]] | ||
[[Category: Domnik, L]] | [[Category: Domnik, L]] | ||
[[Category: Goetzl, S]] | [[Category: Goetzl, S]] | ||
[[Category: Jeoung, J H]] | |||
[[Category: Anaerobiosis]] | |||
[[Category: Carbon dioxide]] | |||
[[Category: Carbon monoxide]] | |||
[[Category: Crystallization]] | |||
[[Category: Iron]] | |||
[[Category: Ligand]] | |||
[[Category: Nickel]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Recombinant protein]] | |||
Revision as of 05:52, 3 January 2018
Carbon Monoxide Dehydrogenase IV from Carboxydothermus hydrogenoformans
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