2lm4 | pdb_00002lm4

Solution NMR Structure of mitochondrial succinate dehydrogenase assembly factor 2 from Saccharomyces cerevisiae, Northeast Structural Genomics Consortium Target YT682A

spinqualitylabelsall models 2lm4, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lm4 is a 1 chain structure with sequence from Saccharomyces cerevisiae s288c. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: EMI5, SDH5, YOL071W (Saccharomyces cerevisiae S288c) Resources: FirstGlance, OCA, RCSB, PDBsum Function [SDHF2_YEAST] Required for insertion of FAD cofactor into SDH1, the catalytic subunit of succinate dehydrogenase (SDH). SDH is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). In is unclear whether it participates in the chemistry of FAD attachment (enzymatic function) or acts as a chaperone that maintains SDH1 in a conformation that is susceptible to autocatalytic FAD attachment. Involved in sporulation. Required for the full activation of the early meiotic inducer IME1. Publication Abstract from PubMed The yeast mitochondrial protein Sdh5 is required for the covalent attachment of flavin adenine dinucleotide (FAD) to protein Sdh1, a subunit of the heterotetrameric enzyme succinate dehydrogenase. The NMR structure of Sdh5 represents the first eukaryotic structure of Pfam family PF03937 and reveals a conserved surface region, which likely represents a putative Sdh1-Sdh5 interaction interface. Point mutations in this region result in the loss of covalent flavinylation of Sdh1. Moreover, chemical shift perturbation measurements showed that Sdh5 does not bind FAD in vitro, indicating that it is not a simple cofactor transporter in vivo. Solution NMR Structure of Yeast Succinate Dehydrogenase Flavinylation Factor Sdh5 Reveals a Putative Sdh1 Binding Site.,Eletsky A, Jeong MY, Kim H, Lee HW, Xiao R, Pagliarini DJ, Prestegard JH, Winge DR, Montelione GT, Szyperski T Biochemistry. 2012 Oct 19. PMID:23062074 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Succinate Dehydrogenase

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