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3b52
From Proteopedia
(Difference between revisions)
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<StructureSection load='3b52' size='340' side='right'caption='[[3b52]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='3b52' size='340' side='right'caption='[[3b52]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3b52]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3b52]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans_Z-2901 Carboxydothermus hydrogenoformans Z-2901]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B52 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=WCC:FE(3)-NI(1)-S(4)+CLUSTER'>WCC</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=WCC:FE(3)-NI(1)-S(4)+CLUSTER'>WCC</scene></td></tr> | |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b52 OCA], [https://pdbe.org/3b52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b52 RCSB], [https://www.ebi.ac.uk/pdbsum/3b52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b52 ProSAT]</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=3b52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b52 OCA], [https://pdbe.org/3b52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b52 RCSB], [https://www.ebi.ac.uk/pdbsum/3b52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b52 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/COOS2_CARHZ COOS2_CARHZ] CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH) (By similarity). | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3b52 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3b52 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Anaerobic CO dehydrogenases catalyze the reversible oxidation of CO to CO2 at a complex Ni-, Fe-, and S-containing metal center called cluster C. We report crystal structures of CO dehydrogenase II from Carboxydothermus hydrogenoformans in three different states. In a reduced state, exogenous CO2 supplied in solution is bound and reductively activated by cluster C. In the intermediate structure, CO2 acts as a bridging ligand between Ni and the asymmetrically coordinated Fe, where it completes the square-planar coordination of the Ni ion. It replaces a water/hydroxo ligand bound to the Fe ion in the other two states. The structures define the mechanism of CO oxidation and CO2 reduction at the Ni-Fe site of cluster C. | ||
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| - | Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase.,Jeoung JH, Dobbek H Science. 2007 Nov 30;318(5855):1461-4. PMID:18048691<ref>PMID:18048691</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3b52" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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*[[Carbon monoxide dehydrogenase 3D structures|Carbon monoxide dehydrogenase 3D structures]] | *[[Carbon monoxide dehydrogenase 3D structures|Carbon monoxide dehydrogenase 3D structures]] | ||
*[[IronâÂÂsulfur proteins|IronâÂÂsulfur proteins]] | *[[IronâÂÂsulfur proteins|IronâÂÂsulfur proteins]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Carboxydothermus hydrogenoformans Z-2901]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Dobbek | + | [[Category: Dobbek H]] |
| - | [[Category: Jeoung | + | [[Category: Jeoung JH]] |
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Current revision
Ni,Fe-CODH-600 mV state + CO2
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