Crystal structure of TFIID TATA-box binding protein

D B Nikolov; S H Hu; J Lin; A Gasch; A Hoffmann; M Horikoshi; N H Chua; R G Roeder; S K Burley

doi:10.1038/360040a0

Crystal structure of TFIID TATA-box binding protein

Nature. 1992 Nov 5;360(6399):40-6. doi: 10.1038/360040a0.

Authors

D B Nikolov¹, S H Hu, J Lin, A Gasch, A Hoffmann, M Horikoshi, N H Chua, R G Roeder, S K Burley

Affiliation

¹ Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021-6399.

PMID: 1436073
DOI: 10.1038/360040a0

Abstract

The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIID tau) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 A resolution. This highly symmetric alpha/beta structure contains a new DNA-binding fold, resembling a molecular 'saddle' that sits astride the DNA. The DNA-binding surface is a curved, antiparallel beta-sheet. When bound to DNA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acid Sequence
Arabidopsis
Computer Simulation
DNA / metabolism
Models, Molecular
Molecular Conformation
Molecular Sequence Data
Molecular Structure
Promoter Regions, Genetic / physiology
Sequence Alignment
Sequence Homology, Amino Acid
TATA Box / physiology
Transcription Factor TFIID
Transcription Factors / chemistry*
Transcriptional Activation / physiology
X-Ray Diffraction

Substances

Transcription Factor TFIID
Transcription Factors
DNA