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6t7j

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Current revision

As-isolated Ni-free crystal structure of carbon monoxide dehydrogenase from Thermococcus sp. AM4 produced without CooC maturase

Structural highlights

6t7j is a 3 chain structure with sequence from Thermococcus sp. AM4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.43Å
Ligands:	, , , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B7R5K0_9EURY CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).[ARBA:ARBA00002452]

Publication Abstract from PubMed

Ni-containing CO-dehydrogenases (CODHs) allow some microorganisms to couple ATP synthesis to CO oxidation, or to use either CO or CO2 as a source of carbon. The recent detailed characterizations of some of them have evidenced a great diversity in terms of catalytic properties and resistance to O2. In an effort to increase the number of available CODHs, we have heterologously produced in Desulfovibrio fructosovorans, purified and characterized the two CooS-type CODHs (CooS1 and CooS2) from the hyperthermophilic archaeon Thermococcus sp. AM4 (Tc). We have also crystallized CooS2, which is coupled in vivo to a hydrogenase. CooS1 and CooS2 are homodimers, and harbour five metalloclusters: two [Ni4Fe-4S] C clusters, two [4Fe-4S] B clusters and one interfacial [4Fe-4S] D cluster. We show that both are dependent on a maturase, CooC1 or CooC2, which is interchangeable. The homologous protein CooC3 does not allow Ni insertion in either CooS. The two CODHs from Tc have similar properties: they can both oxidize and produce CO. The Michaelis constants (Km) are in the microM range for CO and in the mM range (CODH 1) or above (CODH 2) for CO2. Product inhibition is observed only for CO2 reduction, consistent with CO2 binding being much weaker than CO binding. The two enzymes are rather O2 sensitive (similarly to CODH II from Carboxydothermus hydrogenoformans), and react more slowly with O2 than any other CODH for which these data are available.

The two CO-dehydrogenases of Thermococcus sp. AM4.,Benvenuti M, Meneghello M, Guendon C, Jacq-Bailly A, Jeoung JH, Dobbek H, Leger C, Fourmond V, Dementin S Biochim Biophys Acta Bioenerg. 2020 Jul 1;1861(7):148188. doi:, 10.1016/j.bbabio.2020.148188. Epub 2020 Mar 21. PMID:32209322^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Benvenuti M, Meneghello M, Guendon C, Jacq-Bailly A, Jeoung JH, Dobbek H, Leger C, Fourmond V, Dementin S. The two CO-dehydrogenases of Thermococcus sp. AM4. Biochim Biophys Acta Bioenerg. 2020 Jul 1;1861(7):148188. doi:, 10.1016/j.bbabio.2020.148188. Epub 2020 Mar 21. PMID:32209322 doi:http://dx.doi.org/10.1016/j.bbabio.2020.148188

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6t7j"

Categories: Large Structures | Thermococcus sp. AM4 | Dobbek H | Jeoung J-H

@@ Line 3: / Line 3: @@
 <StructureSection load='6t7j' size='340' side='right'caption='[[6t7j]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6t7j]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_sp._am4 Thermococcus sp. am4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T7J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6t7j]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_sp._AM4 Thermococcus sp. AM4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T7J FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MSK:Broken+Fe4S4+cluster'>MSK</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.43&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAM4_1067 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246969 Thermococcus sp. AM4])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MSK:Broken+Fe4S4+cluster'>MSK</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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'>[https://en.wikipedia.org/wiki/Anaerobic_carbon-monoxide_dehydrogenase Anaerobic carbon-monoxide dehydrogenase], with EC number [https://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=6t7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7j OCA], [https://pdbe.org/6t7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t7j RCSB], [https://www.ebi.ac.uk/pdbsum/6t7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7j ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/B7R5K0_9EURY B7R5K0_9EURY]] CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).[ARBA:ARBA00002452]
+[https://www.uniprot.org/uniprot/B7R5K0_9EURY B7R5K0_9EURY] CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).[ARBA:ARBA00002452]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Anaerobic carbon-monoxide dehydrogenase]]
 [[Category: Large Structures]]
-[[Category: Thermococcus sp. am4]]
+[[Category: Thermococcus sp. AM4]]
-[[Category: Dobbek, H]]
+[[Category: Dobbek H]]
-[[Category: Jeoung, J H]]
+[[Category: Jeoung J-H]]
-[[Category: Co dehydrogenase]]
-[[Category: Ni-free cluster c]]
-[[Category: Oxidoreductase]]

6t7j

From Proteopedia

Current revision

As-isolated Ni-free crystal structure of carbon monoxide dehydrogenase from Thermococcus sp. AM4 produced without CooC maturase

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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