2lm4

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

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.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.[1] [2] [3]

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[4]

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

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Citations
5 reviews cite this structure
Protein-mediated assembly of succinate dehydrogenase and its cofactors.
Van et al. (2015)
4 more
16 other articles
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See Also

References

  1. ↑ Deutschbauer AM, Williams RM, Chu AM, Davis RW. Parallel phenotypic analysis of sporulation and postgermination growth in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15530-5. Epub 2002 Nov 13. PMID:12432101 doi:http://dx.doi.org/10.1073/pnas.202604399
  2. ↑ Enyenihi AH, Saunders WS. Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics. 2003 Jan;163(1):47-54. PMID:12586695
  3. ↑ Hao HX, Khalimonchuk O, Schraders M, Dephoure N, Bayley JP, Kunst H, Devilee P, Cremers CW, Schiffman JD, Bentz BG, Gygi SP, Winge DR, Kremer H, Rutter J. SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma. Science. 2009 Aug 28;325(5944):1139-42. Epub 2009 Jul 23. PMID:19628817 doi:http://dx.doi.org/1175689
  4. ↑ Eletsky A, Jeong MY, Kim H, Lee HW, Xiao R, Pagliarini DJ, Prestegard JH, Winge DR, Montelione GT, Szyperski T. Solution NMR Structure of Yeast Succinate Dehydrogenase Flavinylation Factor Sdh5 Reveals a Putative Sdh1 Binding Site. Biochemistry. 2012 Oct 19. PMID:23062074 doi:http://dx.doi.org/10.1021/bi301171u

Contents


PDB ID 2lm4

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