1M6U

Crystal Structure of a Novel DNA-binding domain from Ndt80, a Transcriptional Activator Required for Meiosis in Yeast

Summary for 1M6U

• Entry DOI: 10.2210/pdb1m6u/pdb
• Related: 1M7U
• Descriptor: Ndt80 protein, SULFATE ION (3 entities in total)
• Functional Keywords: transcription activator, yeast protein, dna-binding, meiosis
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P38830
• Total number of polymer chains: 2
• Total formula weight: 62999.16

Authors

Montano, S.P.,Cote, M.L.,Fingerman, I.,Pierce, M.,Vershon, A.K.,Georgiadis, M.M. (deposition date: 2002-07-17, release date: 2002-11-06, Last modification date: 2024-02-14)

Primary citation

Montano, S.P.,Cote, M.L.,Fingerman, I.,Pierce, M.,Vershon, A.K.,Georgiadis, M.M.
Crystal structure of the DNA-binding domain from Ndt80, a transcriptional activator required for meiosis in yeast
Proc.Natl.Acad.Sci.USA, 99:14041-14046, 2002

PubMed Abstract: 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.

PubMed: 12384578
DOI: 10.1073/pnas.222312199

Experimental method

X-RAY DIFFRACTION (2.3 Å)