3vrb

From Proteopedia

(Difference between revisions)

Current revision

Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil and substrate fumarate

Structural highlights

3vrb is a 8 chain structure with sequence from Ascaris suum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.91Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

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^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Amino H, Osanai A, Miyadera H, Shinjyo N, Tomitsuka E, Taka H, Mineki R, Murayama K, Takamiya S, Aoki T, Miyoshi H, Sakamoto K, Kojima S, Kita K. Isolation and characterization of the stage-specific cytochrome b small subunit (CybS) of Ascaris suum complex II from the aerobic respiratory chain of larval mitochondria. Mol Biochem Parasitol. 2003 May;128(2):175-86. PMID:12742584 doi:10.1016/s0166-6851(03)00074-4
↑ Iwata F, Shinjyo N, Amino H, Sakamoto K, Islam MK, Tsuji N, Kita K. Change of subunit composition of mitochondrial complex II (succinate-ubiquinone reductase/quinol-fumarate reductase) in Ascaris suum during the migration in the experimental host. Parasitol Int. 2008 Mar;57(1):54-61. PMID:17933581 doi:10.1016/j.parint.2007.08.002
↑ Kita K, Takamiya S, Furushima R, Ma YC, Suzuki H, Ozawa T, Oya H. Electron-transfer complexes of Ascaris suum muscle mitochondria. III. Composition and fumarate reductase activity of complex II. Biochim Biophys Acta. 1988 Sep 14;935(2):130-40. PMID:2843227 doi:10.1016/0005-2728(88)90210-1
↑ Kuramochi T, Hirawake H, Kojima S, Takamiya S, Furushima R, Aoki T, Komuniecki R, Kita K. Sequence comparison between the flavoprotein subunit of the fumarate reductase (complex II) of the anaerobic parasitic nematode, Ascaris suum and the succinate dehydrogenase of the aerobic, free-living nematode, Caenorhabditis elegans. Mol Biochem Parasitol. 1994 Dec;68(2):177-87. PMID:7739664 doi:10.1016/0166-6851(94)90163-5
↑ Saruta F, Kuramochi T, Nakamura K, Takamiya S, Yu Y, Aoki T, Sekimizu K, Kojima S, Kita K. Stage-specific isoforms of complex II (succinate-ubiquinone oxidoreductase) in mitochondria from the parasitic nematode, Ascaris suum. J Biol Chem. 1995 Jan 13;270(2):928-32. PMID:7822332 doi:10.1074/jbc.270.2.928
↑ Takamiya S, Kita K, Wang H, Weinstein PP, Hiraishi A, Oya H, Aoki T. Developmental changes in the respiratory chain of Ascaris mitochondria. Biochim Biophys Acta. 1993 Feb 8;1141(1):65-74. PMID:8435436 doi:10.1016/0005-2728(93)90190-q
↑ Shimizu H, Osanai A, Sakamoto K, Inaoka DK, Shiba T, Harada S, Kita K. Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum. J Biochem. 2012 Jun;151(6):589-92. Epub 2012 May 9. PMID:22577165 doi:10.1093/jb/mvs051

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3vrb"

@@ Line 5: / Line 5: @@
 <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]] 2.91&#8491;</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=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>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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/Q33862_ASCSU Q33862_ASCSU]
+[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 ==

3vrb

From Proteopedia

Current revision

Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil and substrate fumarate

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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