View source for 8bqi


==W-formate dehydrogenase from Desulfovibrio vulgaris - Soaking with Formate 3 min==
<StructureSection load='8bqi' size='340' side='right'caption='[[8bqi]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8bqi]] 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=8BQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BQI 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]] 2.356&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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=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=8bqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bqi OCA], [https://pdbe.org/8bqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bqi RCSB], [https://www.ebi.ac.uk/pdbsum/8bqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bqi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q72EJ1_NITV2 Q72EJ1_NITV2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metal-dependent formate dehydrogenases (Fdh) catalyze the reversible conversion of CO(2) to formate, with unrivalled efficiency and selectivity. However, the key catalytic aspects of these enzymes remain unknown, preventing us from fully benefiting from their capabilities in terms of biotechnological applications. Here, we report a time-resolved characterization by X-ray crystallography of the Desulfovibrio vulgaris Hildenborough SeCys/W-Fdh during formate oxidation. The results allowed us to model five different intermediate structures and to chronologically map the changes occurring during enzyme reduction. Formate molecules were assigned for the first time to populate the catalytic pocket of a Fdh. Finally, the redox reversibility of DvFdhAB in crystals was confirmed by reduction and reoxidation structural studies.

Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation.,Vilela-Alves G, Manuel RR, Oliveira AR, Pereira IC, Romao MJ, Mota C Int J Mol Sci. 2022 Dec 28;24(1):476. doi: 10.3390/ijms24010476. PMID:36613918<ref>PMID:36613918</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8bqi" style="background-color:#fffaf0;"></div>

==See Also==
*[[Formate dehydrogenase 3D structures|Formate dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Desulfovibrio vulgaris str. Hildenborough]]
[[Category: Large Structures]]
[[Category: Manuel RR]]
[[Category: Mota C]]
[[Category: Oliveira AR]]
[[Category: Pereira IC]]
[[Category: Romao MJ]]
[[Category: Vilela-Alves G]]