3sfe

From Proteopedia

(Difference between revisions)

Revision as of 19:17, 25 December 2014

crystal structure of porcine mitochondrial respiratory complex II bound with oxaloacetate and thiabendazole

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.
Ligands:	, , , , , ,
Related:	1zoy, 1zp0, 3sfd
Activity:	Succinate dehydrogenase (ubiquinone), with EC number 1.3.5.1
Resources:	FirstGlance, OCA, RCSB, PDBsum

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). [DHSA_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] [DHSB_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).

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^[2]

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

References

↑ Huo X, Su D, Wang A, Zhai Y, Xu J, Li X, Bartlam M, Sun F, Rao Z. Preliminary molecular characterization and crystallization of mitochondrial respiratory complex II from porcine heart. FEBS J. 2007 Mar;274(6):1524-9. PMID:17480203 doi:http://dx.doi.org/10.1111/j.1742-4658.2007.05698.x
↑ 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

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/3sfe"

@@ Line 8: / Line 8: @@
 <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=3sfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sfe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sfe RCSB], [http://www.ebi.ac.uk/pdbsum/3sfe PDBsum]</span></td></tr>
 </table>
+== 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/DHSA_PIG DHSA_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/DHSB_PIG DHSB_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).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3sfe

From Proteopedia

Revision as of 19:17, 25 December 2014

crystal structure of porcine mitochondrial respiratory complex II bound with oxaloacetate and thiabendazole

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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