8bql: Difference between revisions
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New page: '''Unreleased structure''' The entry 8bql is ON HOLD Authors: Description: Category: Unreleased Structures |
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==W-formate dehydrogenase from Desulfovibrio vulgaris - Co-crystallized with Formate and Reoxidized by exposure to air for 12 min== | |||
<StructureSection load='8bql' size='340' side='right'caption='[[8bql]], [[Resolution|resolution]] 1.91Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8bql]] 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=8BQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BQL 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]] 1.906Å</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=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=8bql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bql OCA], [https://pdbe.org/8bql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bql RCSB], [https://www.ebi.ac.uk/pdbsum/8bql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bql 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8bql" 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]] | |||
Latest revision as of 10:04, 21 November 2024
W-formate dehydrogenase from Desulfovibrio vulgaris - Co-crystallized with Formate and Reoxidized by exposure to air for 12 minW-formate dehydrogenase from Desulfovibrio vulgaris - Co-crystallized with Formate and Reoxidized by exposure to air for 12 min
Structural highlights
FunctionPublication Abstract from PubMedMetal-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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