5fle
From Proteopedia
(Difference between revisions)
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<StructureSection load='5fle' size='340' side='right' caption='[[5fle]], [[Resolution|resolution]] 1.23Å' scene=''> | <StructureSection load='5fle' size='340' side='right' caption='[[5fle]], [[Resolution|resolution]] 1.23Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5fle]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FLE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fle]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Carhz Carhz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FLE FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=82N:NICKEL+IRON+CLSUTER+WITH+CYANIDE+BOUND'>82N</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></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=82N:NICKEL+IRON+CLSUTER+WITH+CYANIDE+BOUND'>82N</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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5flh|5flh]], [[5fli|5fli]], [[5flj|5flj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5flh|5flh]], [[5fli|5fli]], [[5flj|5flj]]</td></tr> | ||
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== Function == | == Function == | ||
[[http://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). | [[http://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). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Carbon monoxide dehydrogenase (CODH) is a key enzyme for reversible CO interconversion. To elucidate structural and mechanistic details of CO binding at the CODH active site (C-cluster), cyanide is frequently used as an iso-electronic substitute and inhibitor. However, previous studies revealed conflicting results on the structure of the cyanide-bound complex and the mechanism of cyanide-inhibition. To address this issue in this work, we have employed IR spectroscopy, crystallography, site directed mutagenesis, and theoretical methods to analyse the cyanide complex of the CODH from Carboxydothermus hydrogenoformans (CODHII Ch ). IR spectroscopy demonstrates that a single cyanide binds to the Ni ion. Whereas the inhibitor could be partially removed at elevated temperature, irreversible degradation of the C-cluster occurred in the presence of an excess of cyanide on the long-minute time scale, eventually leading to the formation of [Fe(CN)6](4-) and [Ni(CN)4](2-) complexes. Theoretical calculations based on a new high-resolution structure of the cyanide-bound CODHII Ch indicated that cyanide binding to the Ni ion occurs upon dissociation of the hydroxyl ligand from the Fe1 subsite of the C-cluster. The hydroxyl group is presumably protonated by Lys563 which, unlike to His93, does not form a hydrogen bond with the cyanide ligand. A stable deprotonated epsilon-amino group of Lys563 in the cyanide complex is consistent with the nearly unchanged C[triple bond, length as m-dash]N stretching in the Lys563Ala variant of CODHII Ch . These findings support the view that the proton channel connecting the solution phase with the active site displays a strict directionality, controlled by the oxidation state of the C-cluster. | ||
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| + | When the inhibitor tells more than the substrate: the cyanide-bound state of a carbon monoxide dehydrogenase.,Ciaccafava A, Tombolelli D, Domnik L, Fesseler J, Jeoung JH, Dobbek H, Mroginski MA, Zebger I, Hildebrandt P Chem Sci. 2016 May 1;7(5):3162-3171. doi: 10.1039/c5sc04554a. Epub 2016 Jan 27. PMID:29997808<ref>PMID:29997808</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5fle" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Carbon monoxide dehydrogenase|Carbon monoxide dehydrogenase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Carhz]] | ||
[[Category: Ciaccafava, A]] | [[Category: Ciaccafava, A]] | ||
[[Category: Dobbek, H]] | [[Category: Dobbek, H]] | ||
Revision as of 07:46, 29 August 2018
High resolution NI,FE-CODH-320 mV with CN state
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