Co-crystal structure of TBP recognizing the minor groove of a TATA element

Joseph L. Kim, Dimitar B. Nikolov, Stephen K. Burley

Research output: Contribution to journalArticle

915 Citations (Scopus)

Abstract

The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter has been determined by X-ray crystallography at 2.25 Å resolution. Binding of the saddle-shaped protein induces a conformational change in the DNA, inducing sharp kinks at either end of the sequence TATAAAAG. Between the kinks, the right-handed double helix is smoothly curved and partially unwound, presenting a widened minor groove to TBP's concave, antiparallel β-sheet. Side-chain/base interactions are restricted to the minor groove, and include hydrogen bonds, van der Waals contacts and phenylalanine-base stacking interactions.

Original languageEnglish (US)
Pages (from-to)520-527
Number of pages8
JournalNature
Volume365
Issue number6446
DOIs
StatePublished - Jan 1 1993

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TATA Box
X Ray Crystallography
Phenylalanine
Adenoviridae
Hydrogen
Peptides
DNA
Proteins
tributyl phosphate

All Science Journal Classification (ASJC) codes

  • General

Cite this

Kim, Joseph L. ; Nikolov, Dimitar B. ; Burley, Stephen K. / Co-crystal structure of TBP recognizing the minor groove of a TATA element. In: Nature. 1993 ; Vol. 365, No. 6446. pp. 520-527.
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Co-crystal structure of TBP recognizing the minor groove of a TATA element. / Kim, Joseph L.; Nikolov, Dimitar B.; Burley, Stephen K.

In: Nature, Vol. 365, No. 6446, 01.01.1993, p. 520-527.

Research output: Contribution to journalArticle

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