Crystal structure of yeast TATA-binding protein and model for interaction with DNA

The C-terminal 179-aa region of yeast (Saccharomyces cerevisiae) TATA-binding protein (TBP), phylogenetically conserved and sufficient for many functions, formed crystals diffracting to 1.7-angstroms resolution. The structure of the protein, determined by molecular replacement with coordinates from...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1993-09, Vol.90 (17), p.8174-8178
Main Authors: Chasman, Daniel I., Flaherty, Kevin M., Sharp, Phillip A., Kornberg, Roger D.
Format: Article
Language:English
Subjects:
adn
Amino Acid Sequence
Amino acids
Arabidopsis - metabolism
arabidopsis thaliana
Base Sequence
Biochemistry
Biological and medical sciences
Crystal structure
Crystalline structure
Crystallography
Crystals
Deoxyribonucleic acid
DNA
DNA - chemistry
DNA - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Genetic mutation
modele
modelos
Models, Molecular
Models, Structural
Molecular and cellular biology
Molecular biophysics
Molecular genetics
Molecular Sequence Data
Monomers
Phosphates
Protein Structure, Secondary
proteinas
proteine
Proteins
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - metabolism
Sequence Homology, Amino Acid
Structure in molecular biology
TATA Box
TATA-Box Binding Protein
Transcription Factors - chemistry
Transcription Factors - metabolism
Transcription. Transcription factor. Splicing. Rna processing
Wildlife conservation
X-Ray Diffraction
Yeast
Yeasts
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Description
Summary:The C-terminal 179-aa region of yeast (Saccharomyces cerevisiae) TATA-binding protein (TBP), phylogenetically conserved and sufficient for many functions, formed crystals diffracting to 1.7-angstroms resolution. The structure of the protein, determined by molecular replacement with coordinates from Arabidopsis TBP and refined to 2.6 angstroms, differed from that in Arabidopsis slightly by an angle of about 12 degrees between two structurally nearly identical subdomains, indicative of a degree of conformational flexibility. A model for TBP-DNA interaction is proposed with the following important features: the long dimension of the protein follows the trajectory of the minor groove; two rows of basic residues conserved between the subdomains lie along the edges of the protein in proximity to the DNA phosphates; a band of hydrophobic residues runs down the middle of the groove; and amino acid residues whose mutation alters specificity for the second base of the TATA sequence are juxtaposed to that base.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.90.17.8174