1L3G
NMR Structure of the DNA-binding Domain of Cell Cycle Protein, Mbp1(2-124) from Saccharomyces cerevisiae
Summary for 1L3G
| Entry DOI | 10.2210/pdb1l3g/pdb |
| NMR Information | BMRB: 4254 |
| Descriptor | TRANSCRIPTION FACTOR Mbp1 (1 entity in total) |
| Functional Keywords | cell cycle, mlu 1 cell cycle box binding protein, winged helix-turn-helix proteins |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus: P39678 |
| Total number of polymer chains | 1 |
| Total formula weight | 15467.54 |
| Authors | Nair, M.,McIntosh, P.B.,Frenkiel, T.A.,Kelly, G.,Taylor, I.A.,Smerdon, S.J.,Lane, A.N. (deposition date: 2002-02-27, release date: 2003-02-18, Last modification date: 2024-05-22) |
| Primary citation | Nair, M.,McIntosh, P.B.,Frenkiel, T.A.,Kelly, G.,Taylor, I.A.,Smerdon, S.J.,Lane, A.N. NMR Structure of the DNA-Binding Domain of the Cell Cycle Protein Mbp1 from Saccharomyces cerevisiae Biochemistry, 42:1266-1273, 2003 Cited by PubMed Abstract: The three-dimensional solution structure of the DNA-binding domain of Mlu-1 box binding protein (Mbp1) has been determined by multidimensional NMR spectroscopy. Mbp1 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 beta-sheet segment folded against two pairs of alpha-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 beta-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. PubMed: 12564929DOI: 10.1021/bi0205247 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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