1suf
From Proteopedia
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| - | [[Image:1suf.jpg|left|200px]] | + | [[Image:1suf.jpg|left|200px]] |
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| - | '''Carbon Monoxide Dehydrogenase from Carboxydothermus hydrogenoformans-Inactive state''' | + | {{Structure |
| + | |PDB= 1suf |SIZE=350|CAPTION= <scene name='initialview01'>1suf</scene>, resolution 1.15Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> and <scene name='pdbligand=NFS:FE(4)-NI(1)-S(5) CLUSTER'>NFS</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Carbon Monoxide Dehydrogenase from Carboxydothermus hydrogenoformans-Inactive state''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SUF is a [ | + | 1SUF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUF OCA]. |
==Reference== | ==Reference== | ||
| - | Carbon monoxide induced decomposition of the active site [Ni-4Fe-5S] cluster of CO dehydrogenase., Dobbek H, Svetlitchnyi V, Liss J, Meyer O, J Am Chem Soc. 2004 May 5;126(17):5382-7. PMID:[http:// | + | Carbon monoxide induced decomposition of the active site [Ni-4Fe-5S] cluster of CO dehydrogenase., Dobbek H, Svetlitchnyi V, Liss J, Meyer O, J Am Chem Soc. 2004 May 5;126(17):5382-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15113209 15113209] |
[[Category: Carbon-monoxide dehydrogenase (acceptor)]] | [[Category: Carbon-monoxide dehydrogenase (acceptor)]] | ||
[[Category: Carboxydothermus hydrogenoformans]] | [[Category: Carboxydothermus hydrogenoformans]] | ||
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[[Category: nickel]] | [[Category: nickel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:09:45 2008'' |
Revision as of 12:09, 20 March 2008
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| , resolution 1.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Carbon-monoxide dehydrogenase (acceptor), with EC number 1.2.99.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Carbon Monoxide Dehydrogenase from Carboxydothermus hydrogenoformans-Inactive state
Overview
During the past two years, crystal structures of Cu- and Mo-containing carbon monoxide dehydrogenases (CODHs) and Ni- and Fe-containing CODHs have been reported. The active site of CODHs from anaerobic bacteria (cluster C) is composed of Ni, Fe, and S for which crystallographic studies of the enzymes from Carboxydothermus hydrogenoformans, Rhodospirillum rubrum, and Moorella thermoaceticarevealed structural similarities in the overall protein fold but showed substantial differences in the essential Ni coordination environment. The [Ni-4Fe-5S] cluster C in the fully catalytically competent dithionite-reduced CODH II from C. hydrogenoformans (CODHII(Ch)) at 1.6 A resolution contains a characteristic mu(2)-sulfido ligand between Ni and Fe1, resulting in a square-planar ligand arrangement with four S-ligands at the Ni ion. In contrast, the [Ni-4Fe-4S] clusters C in CO-treated CODH from R. rubrum resolved at 2.8 A and in CO-treated acetyl-CoA synthase/CODH complex from M. thermoacetica at 2.2 and 1.9 A resolution, respectively, do not contain the mu(2)-sulfido ligand between Ni and Fe1 and display dissimilar geometries at the Ni ion. The [Ni-4Fe-4S] cluster is composed of a cubane [Ni-3Fe-4S] cluster linked to a mononuclear Fe site. The described coordination geometries of the Ni ion in the [Ni-4Fe-4S] cluster of R. rubrum and M. thermoacetica deviate from the square-planar ligand geometry in the [Ni-4Fe-5S] cluster C of CODHII(Ch). In addition, the latter was converted into a [Ni-4Fe-4S] cluster under specific conditions. The objective of this study was to elucidate the relationship between the structure of cluster C in CODHII(Ch) and the functionality of the protein. We have determined the CO oxidation activity of CODHII(Ch) under different conditions of crystallization, prepared crystals of the enzyme in the presence of dithiothreitol or dithionite as reducing agents under an atmosphere of N(2) or CO, and solved the corresponding structures at 1.1 to 1.6 A resolutions. Fully active CODHII(Ch) obtained after incubation of the enzyme with dithionite under N(2) revealed the [Ni-4Fe-5S] cluster. Short treatment of the enzyme with CO in the presence of dithiothreitol resulted in a catalytically competent CODHII(Ch) with a CO-reduced [Ni-4Fe-5S] cluster, but a prolonged treatment with CO caused the loss of CO-oxidizing activity and revealed a [Ni-4Fe-4S] cluster, which did not contain a mu(2)-S. These data suggest that the [Ni-4Fe-4S] cluster of CODHII(Ch) is an inactivated decomposition product originating from the [Ni-4Fe-5S] cluster.
About this Structure
1SUF is a Single protein structure of sequence from Carboxydothermus hydrogenoformans. Full crystallographic information is available from OCA.
Reference
Carbon monoxide induced decomposition of the active site [Ni-4Fe-5S] cluster of CO dehydrogenase., Dobbek H, Svetlitchnyi V, Liss J, Meyer O, J Am Chem Soc. 2004 May 5;126(17):5382-7. PMID:15113209
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