7z5o: Difference between revisions

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<table><tr><td colspan='2'>[[7z5o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._Hildenborough Desulfovibrio vulgaris str. Hildenborough]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z5O FirstGlance]. <br>
<table><tr><td colspan='2'>[[7z5o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._Hildenborough Desulfovibrio vulgaris str. Hildenborough]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z5O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.527&#8491;</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]] 1.527&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=W:TUNGSTEN+ION'>W</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=W:TUNGSTEN+ION'>W</scene></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=7z5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z5o OCA], [https://pdbe.org/7z5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z5o RCSB], [https://www.ebi.ac.uk/pdbsum/7z5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z5o 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=7z5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z5o OCA], [https://pdbe.org/7z5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z5o RCSB], [https://www.ebi.ac.uk/pdbsum/7z5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z5o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q72EJ1_DESVH Q72EJ1_DESVH]  
[https://www.uniprot.org/uniprot/Q72EJ0_NITV2 Q72EJ0_NITV2]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metal-dependent formate dehydrogenases are important enzymes due to their activity of CO2 reduction to formate. The tungsten-containing FdhAB formate dehydrogenase from Desulfovibrio vulgaris Hildenborough is a good example displaying high activity, simple composition, and a notable structural and catalytic robustness. Here, we report the first spectroscopic redox characterization of FdhAB metal centers by EPR. Titration with dithionite or formate leads to reduction of three [4Fe-4S](1+) clusters, and full reduction requires Ti(III)-citrate. The redox potentials of the four [4Fe-4S](1+) centers range between -250 and -530 mV. Two distinct W(V) signals were detected, WD(V) and WF(V), which differ in only the g2-value. This difference can be explained by small variations in the twist angle of the two pyranopterins, as determined through DFT calculations of model compounds. The redox potential of W(VI/V) was determined to be -370 mV when reduced by dithionite and -340 mV when reduced by formate. The crystal structure of dithionite-reduced FdhAB was determined at high resolution (1.5 A), revealing the same structural alterations as reported for the formate-reduced structure. These results corroborate a stable six-ligand W coordination in the catalytic intermediate W(V) state of FdhAB.
 
Spectroscopic and Structural Characterization of Reduced Desulfovibrio vulgaris Hildenborough W-FdhAB Reveals Stable Metal Coordination during Catalysis.,Oliveira AR, Mota C, Klymanska K, Biaso F, Romao MJ, Guigliarelli B, Pereira IC ACS Chem Biol. 2022 Jul 15;17(7):1901-1909. doi: 10.1021/acschembio.2c00336. Epub, 2022 Jun 29. PMID:35766974<ref>PMID:35766974</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7z5o" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Formate dehydrogenase 3D structures|Formate dehydrogenase 3D structures]]
*[[Formate dehydrogenase 3D structures|Formate dehydrogenase 3D structures]]
== References ==
<references/>
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Retrieved from "https://proteopedia.org/7z5o"