title: Crystal structure of the DNA-binding domain of Mbp1, a transcription factor important in cell-cycle control of DNA synthesis.
abstract: BACKGROUND
  During the cell cycle, cells progress through four distinct phases, G1, S, G2 and M; transcriptional controls play an important role at the transition between these phases. MCB-binding factor (MBF), a transcription factor from budding yeast, binds to the so-called MCB (MluI cell-cycle box) elements found in the promoters of many DNA synthesis genes, and activates the transcription of those at the G1-->S phase transition. MBF is comprised of two proteins, Mbp1 and Swi6.
  
  
  RESULTS
  The three-dimensional structure of the N-terminal DNA-binding domain of Mbp1 has been determined by multiwavelength anomalous diffraction from crystals of the selenomethionyl variant of the protein. The structure is composed of a six-stranded beta sheet interspersed with two pairs of alpha helices. The most conserved core region among Mbp1-related transcription factors folds into a central helix-turn-helix motif with a short N-terminal beta strand and a C-terminal beta hairpin.
  
  
  CONCLUSIONS
  Despite little sequence similarity, the structure within the core region of the Mbp1 N-terminal domain exhibits a similar fold to that of the DNA-binding domains of other proteins, such as hepatocyte nuclear factor-3gamma and histone H5 from eukaryotes, and the prokaryotic catabolite gene activator. However, the structure outside the core region defines Mbp1 as a larger entity with substructures that stabilize and display the helix-turn-helix motif.
authors.affiliation: WM Keck Structural Biology Laboratory Cold Spring Harbor Laboratory Cold Spring Harbor New York, 11724, USA.
authors.forename: R M
authors.initials: RM
authors.lastname: Xu
authors.forename: C
authors.initials: C
authors.lastname: Koch
authors.forename: Y
authors.initials: Y
authors.lastname: Liu
authors.forename: J R
authors.initials: JR
authors.lastname: Horton
authors.forename: D
authors.initials: D
authors.lastname: Knapp
authors.forename: K
authors.initials: K
authors.lastname: Nasmyth
authors.forename: X
authors.initials: X
authors.lastname: Cheng
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002453:Cell Cycle; D018360:Crystallography, X-Ray; D004261:DNA Replication / Q000502:physiology*; D004271:DNA, Fungal / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D019077:Helix-Turn-Helix Motifs; D051543:Hepatocyte Nuclear Factor 3-gamma; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000737:chemistry; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism
chemical_list: D004271:DNA, Fungal; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; C083209:MBP1 protein, S cerevisiae; D009687:Nuclear Proteins; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D051543:Hepatocyte Nuclear Factor 3-gamma