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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[3sfe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SFE FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3sfe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SFE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TMG:2-(1,3-THIAZOL-4-YL)-1H-BENZIMIDAZOLE'>TMG</scene></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]] 2.81Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zoy|1zoy]], [[1zp0|1zp0]], [[3sfd|3sfd]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=TMG:2-(1,3-THIAZOL-4-YL)-1H-BENZIMIDAZOLE'>TMG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Succinate_dehydrogenase_(quinone) Succinate dehydrogenase (quinone)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.1 1.3.5.1] </span></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sfe OCA], [https://pdbe.org/3sfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sfe RCSB], [https://www.ebi.ac.uk/pdbsum/3sfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sfe 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=3sfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sfe OCA], [https://pdbe.org/3sfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sfe RCSB], [https://www.ebi.ac.uk/pdbsum/3sfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sfe ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/DHSD_PIG DHSD_PIG]] Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). [[https://www.uniprot.org/uniprot/SDHA_PIG SDHA_PIG]] Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor (By similarity). [[https://www.uniprot.org/uniprot/C560_PIG C560_PIG]] Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).<ref>PMID:17480203</ref> [[https://www.uniprot.org/uniprot/SDHB_PIG SDHB_PIG]] Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
| + | [https://www.uniprot.org/uniprot/SDHA_PIG SDHA_PIG] Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Sus scrofa]] | | [[Category: Sus scrofa]] |
| - | [[Category: Liu, M]] | + | [[Category: Liu M]] |
| - | [[Category: Sun, F]] | + | [[Category: Sun F]] |
| - | [[Category: Zhai, Y J]] | + | [[Category: Zhai YJ]] |
| - | [[Category: Zhou, Q J]] | + | [[Category: Zhou QJ]] |
| - | [[Category: Oxidoreductase]]
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| - | [[Category: Succinate:ubiquinone oxidoreductase]]
| + | |
| - | [[Category: Thiabendazole]]
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| Structural highlights
3sfe is a 4 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.81Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
SDHA_PIG Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor (By similarity).
Publication Abstract from PubMed
The mitochondrial respiratory complex II or succinate: ubiquinone oxidoreductase (SQR) is a key membrane complex in both the tricarboxylic acid cycle and aerobic respiration. Five disinfectant compounds were investigated with their potent inhibition effects on the ubiquinone reduction activity of the porcine mitochondrial SQR by enzymatic assay and crystallography. Crystal structure of the SQR bound with thiabendazole (TBZ) reveals a different inhibitor-binding feature at the ubiquinone binding site where a water molecule plays an important role. The obvious inhibitory effect of TBZ based on the biochemical data (IC(50) approximately 100 mumol/L) and the significant structure-based binding affinity calculation ( approximately 94 mumol/L) draw the suspicion of using TBZ as a good disinfectant compound for nematode infections treatment and fruit storage.
Thiabendazole inhibits ubiquinone reduction activity of mitochondrial respiratory complex II via a water molecule mediated binding feature.,Zhou Q, Zhai Y, Lou J, Liu M, Pang X, Sun F Protein Cell. 2011 Jul;2(7):531-42. Epub 2011 Aug 6. PMID:21822798[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhou Q, Zhai Y, Lou J, Liu M, Pang X, Sun F. Thiabendazole inhibits ubiquinone reduction activity of mitochondrial respiratory complex II via a water molecule mediated binding feature. Protein Cell. 2011 Jul;2(7):531-42. Epub 2011 Aug 6. PMID:21822798 doi:10.1007/s13238-011-1079-1
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