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| | <StructureSection load='3ae9' size='340' side='right'caption='[[3ae9]], [[Resolution|resolution]] 3.31Å' scene=''> | | <StructureSection load='3ae9' size='340' side='right'caption='[[3ae9]], [[Resolution|resolution]] 3.31Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ae9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AE9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ae9]] 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=3AE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AE9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FD8:N-[3-(PENTAFLUOROPHENOXY)PHENYL]-2-(TRIFLUOROMETHYL)BENZAMIDE'>FD8</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 3.31Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3abv|3abv]], [[3ae1|3ae1]], [[3ae2|3ae2]], [[3ae3|3ae3]], [[3ae4|3ae4]], [[3ae5|3ae5]], [[3ae6|3ae6]], [[3ae7|3ae7]], [[3ae8|3ae8]], [[3aea|3aea]], [[3aeb|3aeb]], [[3aec|3aec]], [[3aed|3aed]], [[3aee|3aee]], [[3aef|3aef]], [[3aeg|3aeg]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FD8:N-[3-(PENTAFLUOROPHENOXY)PHENYL]-2-(TRIFLUOROMETHYL)BENZAMIDE'>FD8</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ae9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ae9 OCA], [https://pdbe.org/3ae9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ae9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ae9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ae9 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=3ae9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ae9 OCA], [https://pdbe.org/3ae9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ae9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ae9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ae9 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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pig]] | + | [[Category: Sus scrofa]] |
| - | [[Category: Harada, S]] | + | [[Category: Harada S]] |
| - | [[Category: Honma, T]] | + | [[Category: Honma T]] |
| - | [[Category: Inaoka, D K]] | + | [[Category: Inaoka DK]] |
| - | [[Category: Inoue, M]] | + | [[Category: Inoue M]] |
| - | [[Category: Kido, Y]] | + | [[Category: Kido Y]] |
| - | [[Category: Kita, K]] | + | [[Category: Kita K]] |
| - | [[Category: Mao, J]] | + | [[Category: Mao J]] |
| - | [[Category: Matsuoka, S]] | + | [[Category: Matsuoka S]] |
| - | [[Category: Omori, J]] | + | [[Category: Omori J]] |
| - | [[Category: Osanai, A]] | + | [[Category: Osanai A]] |
| - | [[Category: Sakamoto, K]] | + | [[Category: Sakamoto K]] |
| - | [[Category: Sasaki, T]] | + | [[Category: Sasaki T]] |
| - | [[Category: Shindo, M]] | + | [[Category: Shindo M]] |
| - | [[Category: Tanaka, A]] | + | [[Category: Tanaka A]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Fad-binding protein]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Iron-sulfur]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Mitochondrion]]
| + | |
| - | [[Category: Mitochondrion inner membrane]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
| + | |
| - | [[Category: Respiratory complex ii]]
| + | |
| - | [[Category: Transit peptide]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Tricarboxylic acid cycle]]
| + | |
| Structural highlights
3ae9 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 3.31Å |
| 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
Recent studies on the respiratory chain of Ascaris suum showed that the mitochondrial NADH-fumarate reductase system composed of complex I, rhodoquinone and complex II plays an important role in the anaerobic energy metabolism of adult A. suum. The system is the major pathway of energy metabolism for adaptation to a hypoxic environment not only in parasitic organisms, but also in some types of human cancer cells. Thus, enzymes of the pathway are potential targets for chemotherapy. We found that flutolanil is an excellent inhibitor for A. suum complex II (IC50 = 0.058 muM) but less effectively inhibits homologous porcine complex II (IC50 = 45.9 muM). In order to account for the specificity of flutolanil to A. suum complex II from the standpoint of structural biology, we determined the crystal structures of A. suum and porcine complex IIs binding flutolanil and its derivative compounds. The structures clearly demonstrated key interactions responsible for its high specificity to A. suum complex II and enabled us to find analogue compounds, which surpass flutolanil in both potency and specificity to A. suum complex II. Structures of complex IIs binding these compounds will be helpful to accelerate structure-based drug design targeted for complex IIs.
Structural Insights into the Molecular Design of Flutolanil Derivatives Targeted for Fumarate Respiration of Parasite Mitochondria.,Inaoka DK, Shiba T, Sato D, Balogun EO, Sasaki T, Nagahama M, Oda M, Matsuoka S, Ohmori J, Honma T, Inoue M, Kita K, Harada S Int J Mol Sci. 2015 Jul 7;16(7):15287-308. doi: 10.3390/ijms160715287. PMID:26198225[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Inaoka DK, Shiba T, Sato D, Balogun EO, Sasaki T, Nagahama M, Oda M, Matsuoka S, Ohmori J, Honma T, Inoue M, Kita K, Harada S. Structural Insights into the Molecular Design of Flutolanil Derivatives Targeted for Fumarate Respiration of Parasite Mitochondria. Int J Mol Sci. 2015 Jul 7;16(7):15287-308. doi: 10.3390/ijms160715287. PMID:26198225 doi:http://dx.doi.org/10.3390/ijms160715287
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