2KM1

Solution structure of the N-terminal domain of the yeast protein Dre2

Summary for 2KM1

• Entry DOI: 10.2210/pdb2km1/pdb
• Descriptor: Protein DRE2 (1 entity in total)
• Functional Keywords: dre2, yeast, antiapoptotic, protein binding
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasm: P36152
• Total number of polymer chains: 1
• Total formula weight: 15140.46

Authors

Craescu, C.T.,Soler, N.,Delagoutte, E.,Baldacci, G.,Vernis-Beringue, L. (deposition date: 2009-07-16, release date: 2010-08-11, Last modification date: 2024-05-01)

Primary citation

Soler, N.,Craescu, C.T.,Gallay, J.,Frapart, Y.M.,Mansuy, D.,Raynal, B.,Baldacci, G.,Pastore, A.,Huang, M.E.,Vernis, L.
A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S containing yeast protein Dre2
Febs J., 2012

PubMed Abstract: 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 cytokine-induced apoptosis inhibitor 1 (also known as 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 methyltransferase fold lacking two α-helices and a β-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 the C-terminus domain in vivo.

PubMed: 22487307
DOI: 10.1111/j.1742-4658.2012.08597.x

Experimental method

SOLUTION NMR