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PMID: 8367480 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 17 ·1993-09-01 ·Pages 8174-8

Chasman DI, Flaherty KM, Sharp PA, Kornberg RD

Abstract

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-A resolution. The structure of the protein, determined by molecular replacement with coordinates from Arabidopsis TBP and refined to 2.6 A, 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.

MeSH Terms
Amino Acid Sequence Arabidopsis/metabolism Base Sequence DNA/chemistry,metabolism DNA-Binding Proteins/chemistry,metabolism Escherichia coli/genetics Models, Molecular Models, Structural Molecular Sequence Data Protein Structure, Secondary Recombinant Proteins/chemistry,metabolism Saccharomyces cerevisiae/metabolism Sequence Homology, Amino Acid TATA Box TATA-Box Binding Protein Transcription Factors/chemistry,metabolism X-Ray Diffraction
Chemicals
DNA-Binding Proteins Recombinant Proteins TATA-Box Binding Protein Transcription Factors DNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Chasman D I
Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.
Flaherty K M
Sharp P A
Kornberg R D
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35 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.17.8174
Published
1993-09-01
Pages
8174-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC47311
Subset
IM
Grants
NIAID NIH HHS · AI21144 · United States
NIGMS NIH HHS · GM3992 · United States
NCI NIH HHS · P01-CA42063 · United States
External Links
PubMed source DOI: 10.1073/pnas.90.17.8174 PMC Full Text View journal details
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