3vrb
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3vrb is ON HOLD Authors: Shimizu, H., Shiba, T., Inaoka, D.K., Osanai, A., Kita, K., Sakamoto, K., Harada, S. Description: Mitochondrial rhodoquino...) |
|||
(10 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | + | ==Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil and substrate fumarate== | |
+ | <StructureSection load='3vrb' size='340' side='right'caption='[[3vrb]], [[Resolution|resolution]] 2.91Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3vrb]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VRB 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]] 2.91Å</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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FTN:N-[3-(1-METHYLETHOXY)PHENYL]-2-(TRIFLUOROMETHYL)BENZAMIDE'>FTN</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=3vrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vrb OCA], [https://pdbe.org/3vrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vrb RCSB], [https://www.ebi.ac.uk/pdbsum/3vrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vrb ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/SDHA1_ASCSU SDHA1_ASCSU] Flavoprotein (Fp) subunit of the mitochondrial electron transport chain complex II which, together with the iron-sulfur protein (Ip) subunit forms the catalytic core of the complex (PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7739664, PubMed:7822332, PubMed:8435436). During the parasitic larvae and adult stages, which occur in an anaerobic environment, acts as a fumarate reductase by transferring electrons from rhodoquinol to fumarate (PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7739664, PubMed:7822332, PubMed:8435436).<ref>PMID:12742584</ref> <ref>PMID:17933581</ref> <ref>PMID:2843227</ref> <ref>PMID:7739664</ref> <ref>PMID:7822332</ref> <ref>PMID:8435436</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | In the anaerobic respiratory chain of the parasitic nematode Ascaris suum, complex II couples the reduction of fumarate to the oxidation of rhodoquinol, a reverse reaction catalyzed by mammalian complex II. In this study, the first structure of anaerobic complex II of mitochondria was determined. The structure, composed of four subunits and five co-factors, is similar to that of aerobic complex II, except for an extra peptide found in the smallest anchor subunit of the A. suum enzyme. We discuss herein the structure-function relationship of the enzyme and the critical role of the low redox potential of rhodoquinol in the fumarate reduction of A. suum complex II. | ||
- | + | Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum.,Shimizu H, Osanai A, Sakamoto K, Inaoka DK, Shiba T, Harada S, Kita K J Biochem. 2012 Jun;151(6):589-92. Epub 2012 May 9. PMID:22577165<ref>PMID:22577165</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 3vrb" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Ascaris suum]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Harada S]] | ||
+ | [[Category: Inaoka DK]] | ||
+ | [[Category: Kita K]] | ||
+ | [[Category: Osanai A]] | ||
+ | [[Category: Sakamoto K]] | ||
+ | [[Category: Shiba T]] | ||
+ | [[Category: Shimizu H]] |
Current revision
Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil and substrate fumarate
|
Categories: Ascaris suum | Large Structures | Harada S | Inaoka DK | Kita K | Osanai A | Sakamoto K | Shiba T | Shimizu H