NMR structure of the DNA-binding domain of the cell cycle protein Mbp1 from Saccharomyces cerevisiae

Margie Nair, Pauline B. McIntosh, Thomas A. Frenkiel, Geoff Kelly, Ian A. Taylor, Stephen J. Smerdon, Andrew N. Lane

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


The three-dimensional solution structure of the DNA-binding domain of Mlu-1 box binding protein (Mbp1) has been determined by multidimensional NMR spectroscopy. Mbpl is a cell cycle transcription factor from Saccharomyces cerevisiae and consists of an N-terminal DNA-binding domain, a series of ankyrin repeats, and a heterodimerization domain at the C-terminus. A set of conformers comprising 19 refined structures was calculated via a molecular dynamics simulated annealing protocol using distance, dihedral angle, and residual dipolar coupling restraints derived from either double or triple resonance NMR experiments. The solution structure consists of a six-stranded β-sheet segment folded against two pairs of α-helices in the topology of the winged helix-turn-helix family of proteins and is in agreement with the X-ray structures. In addition, the solution structure shows that the C-terminal tail region of this domain folds back and makes specific interactions with the N-terminal β-strand of the protein. This C-terminal region is essential for full DNA-binding activity but appears in the X-ray structure to be disordered. The fold-back structure extends the region of positive electrostatic potential, and this may enhance the nonspecific contribution to binding by favorable electrostatic interactions with the DNA backbone.

Original languageEnglish
Pages (from-to)1266-1273
Number of pages8
Issue number5
StatePublished - Feb 11 2003

ASJC Scopus subject areas

  • Biochemistry


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