1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG

Joseph L. Kim, Stephen K. Burley

Research output: Contribution to journalArticle

193 Scopus citations

Abstract

The three-dimensional structure of a TATA box-binding protein (TBP) from Arabidopsis thaliana complexed with a fourteen base pair oligonucleotide bearing the Adenovirus major late promoter TATA element has been refined at 1.9 Å resolution, giving a final crystallographic R-factor of 19.4%. Binding of the monomeric, saddle-shaped α/β protein induces an unprecedented conformational change in the DNA. A detailed structural and functional analysis of this unusual protein-DNA complex is presented, with particular emphasis on the mechanisms of DNA deformation, TATA element recognition, and preinitiation complex assembly.

Original languageEnglish (US)
Pages (from-to)638-653
Number of pages16
JournalNature structural biology
Volume1
Issue number9
DOIs
StatePublished - Sep 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics

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