Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Yeast Dre2 is an essential Fe-S cluster-containing protein that has been implicated in cytosolic Fe-S protein biogenesis and in cell death regulation in response to oxidative stress. Its absence in yeast can be complemented by the human homologous antiapoptotic protein Ciapin1/Anamorsin, suggesting at least one common function. Using complementary techniques, we have investigated the biochemical and biophysical properties of Dre2. We show that it contains an N-terminal domain whose structure in solution consists of a stable well-structured monomer with an overall typical S-adenosylmethionine (SAM) methyltransferase fold that however lacks two alpha helices and a beta strand. The highly conserved C-terminus of Dre2, containing two Fe-S clusters, influences the flexibility of the N-terminal domain. We discuss the hypotheses that the activity of the N-terminal domain could be modulated by the redox activity of Fe-S clusters-containing C-terminus domain in vivo.
A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S containing yeast protein Dre2.,Soler N, Craescu CT, Gallay J, Frapart YM, Mansuy D, Raynal B, Baldacci G, Pastore A, Huang ME, Vernis L FEBS J. 2012 Apr 9. doi: 10.1111/j.1742-4658.2012.08597.x. PMID:22487307[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Soler N, Craescu CT, Gallay J, Frapart YM, Mansuy D, Raynal B, Baldacci G, Pastore A, Huang ME, Vernis L. A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S containing yeast protein Dre2. FEBS J. 2012 Apr 9. doi: 10.1111/j.1742-4658.2012.08597.x. PMID:22487307 doi:10.1111/j.1742-4658.2012.08597.x
