Crystal structure of the DNA-binding domain of Mbp1, a transcription factor important in cell-cycle control of DNA synthesis

Xu, R. M., Koch, C., Liu, Y., Horton, J. R., Knapp, D., Nasmyth, K., Cheng, X. (March 1997) Crystal structure of the DNA-binding domain of Mbp1, a transcription factor important in cell-cycle control of DNA synthesis. Structure, 5 (3). pp. 349-58. ISSN 0969-2126 (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/9083114
DOI: 10.1016/S0969-2126(97)00192-5

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.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Binding Sites Cell Cycle Comparative Study Crystallography, X-Ray DNA Replication/ physiology DNA, Fungal/ metabolism DNA-Binding Proteins/chemistry Fungal Proteins/ chemistry/metabolism Helix-Turn-Helix Motifs Hepatocyte Nuclear Factor 3-gamma Models, Molecular Molecular Sequence Data Nuclear Proteins/chemistry Protein Binding Protein Conformation Recombinant Fusion Proteins/chemistry Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Saccharomyces cerevisiae/chemistry Saccharomyces cerevisiae Proteins Sequence Alignment Sequence Homology, Amino Acid Transcription Factors/ chemistry/metabolism
Subjects: organism description > yeast > Saccharomyces
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > cell cycle
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Xu lab
Depositing User: Kathleen Darby
Date: 15 March 1997
Date Deposited: 08 May 2014 16:50
Last Modified: 08 May 2014 16:50
Related URLs:
URI: https://repository.cshl.edu/id/eprint/29976

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