3sfe
From Proteopedia
crystal structure of porcine mitochondrial respiratory complex II bound with oxaloacetate and thiabendazole
Structural highlights
FunctionSDHA_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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Large Structures | Sus scrofa | Liu M | Sun F | Zhai YJ | Zhou QJ
