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==Crystal structure of porcine heart mitochondrial complex II with an empty quinone-binding pocket== | ==Crystal structure of porcine heart mitochondrial complex II with an empty quinone-binding pocket== | ||
<StructureSection load='3aef' size='340' side='right' caption='[[3aef]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3aef' size='340' side='right' caption='[[3aef]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3abv|3abv]], [[3ae1|3ae1]], [[3ae2|3ae2]], [[3ae3|3ae3]], [[3ae4|3ae4]], [[3ae5|3ae5]], [[3ae6|3ae6]], [[3ae7|3ae7]], [[3ae8|3ae8]], [[3ae9|3ae9]], [[3aea|3aea]], [[3aeb|3aeb]], [[3aec|3aec]], [[3aed|3aed]], [[3aee|3aee]], [[3aeg|3aeg]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3abv|3abv]], [[3ae1|3ae1]], [[3ae2|3ae2]], [[3ae3|3ae3]], [[3ae4|3ae4]], [[3ae5|3ae5]], [[3ae6|3ae6]], [[3ae7|3ae7]], [[3ae8|3ae8]], [[3ae9|3ae9]], [[3aea|3aea]], [[3aeb|3aeb]], [[3aec|3aec]], [[3aed|3aed]], [[3aee|3aee]], [[3aeg|3aeg]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase_( | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase_(quinone) Succinate dehydrogenase (quinone)], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aef OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aef RCSB], [http://www.ebi.ac.uk/pdbsum/3aef PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aef OCA], [http://pdbe.org/3aef PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aef RCSB], [http://www.ebi.ac.uk/pdbsum/3aef PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aef ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://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). [[http://www.uniprot.org/uniprot/ | [[http://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). [[http://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). [[http://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> [[http://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). | ||
==See Also== | ==See Also== |
Revision as of 06:11, 5 August 2016
Crystal structure of porcine heart mitochondrial complex II with an empty quinone-binding pocketCrystal structure of porcine heart mitochondrial complex II with an empty quinone-binding pocket
Structural highlights
Function[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). [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). [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).[1] [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). See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Sus scrofa
- Harada, S
- Honma, T
- Inaoka, D K
- Inoue, M
- Kido, Y
- Kita, K
- Mao, J
- Matsuoka, S
- Omori, J
- Osanai, A
- Sakamoto, K
- Sasaki, T
- Shindo, M
- Tanaka, A
- Electron transport
- Fad-binding protein
- Heme
- Inhibitor
- Iron
- Iron-sulfur
- Metal-binding
- Mitochondrion
- Mitochondrion inner membrane
- Oxidoreductase
- Respiratory complex ii
- Transit peptide
- Transmembrane
- Transport
- Tricarboxylic acid cycle