Publication Abstract from PubMed
Ndt80 is a transcriptional activator required for meiosis in the yeast Saccharomyces cerevisiae. Here, we report the crystal structure at 2.3 A resolution of the DNA-binding domain of Ndt80 experimentally phased by using the anomalous and isomorphous signal from a single ordered Se atom per molecule of 272-aa residues. The structure reveals a single approximately 32-kDa domain with a distinct fold comprising a beta-sandwich core elaborated with seven additional beta-sheets and three short alpha-helices. Inspired by the structure, we have performed a mutational analysis and defined a DNA-binding motif in this domain. The DNA-binding domain of Ndt80 is homologous to a number of proteins from higher eukaryotes, and the residues that we have shown are required for DNA binding by Ndt80 are highly conserved among this group of proteins. These results suggest that Ndt80 is the defining member of a previously uncharacterized family of transcription factors, including the human protein (C11orf9), which has been shown to be highly expressed in invasive or metastatic tumor cells.
Crystal structure of the DNA-binding domain from Ndt80, a transcriptional activator required for meiosis in yeast.,Montano SP, Cote ML, Fingerman I, Pierce M, Vershon AK, Georgiadis MM Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14041-6. Epub 2002 Oct 16. PMID:12384578[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
