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| | <StructureSection load='6elq' size='340' side='right'caption='[[6elq]], [[Resolution|resolution]] 2.52Å' scene=''> | | <StructureSection load='6elq' size='340' side='right'caption='[[6elq]], [[Resolution|resolution]] 2.52Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6elq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-161 Atcc baa-161]. 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> | + | <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='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> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cooSIV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=129958 ATCC BAA-161])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[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> |
| - | <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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q3AE44_CARHZ Q3AE44_CARHZ] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anaerobic carbon-monoxide dehydrogenase]] | + | [[Category: Carboxydothermus hydrogenoformans]] |
| - | [[Category: Atcc baa-161]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dobbek, H]] | + | [[Category: Dobbek H]] |
| - | [[Category: Domnik, L]] | + | [[Category: Domnik L]] |
| - | [[Category: Goetzl, S]] | + | [[Category: Goetzl S]] |
| - | [[Category: Jeoung, J H]] | + | [[Category: Jeoung JH]] |
| - | [[Category: Anaerobiosis]]
| + | |
| - | [[Category: Carbon dioxide]]
| + | |
| - | [[Category: Carbon monoxide]]
| + | |
| - | [[Category: Crystallization]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Ligand]]
| + | |
| - | [[Category: Nickel]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Recombinant protein]]
| + | |
| Structural highlights
Function
Q3AE44_CARHZ
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Domnik L, Merrouch M, Goetzl S, Jeoung JH, Leger C, Dementin S, Fourmond V, Dobbek H. CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2. Angew Chem Int Ed Engl. 2017 Nov 27;56(48):15466-15469. doi:, 10.1002/anie.201709261. Epub 2017 Nov 2. PMID:29024326 doi:http://dx.doi.org/10.1002/anie.201709261
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