The three-dimensional structure of trp repressor

Richard W. Schevitz, Zdzislaw Otwinowski, Andrzej Joachimiak, Catherine L. Lawson, Paul B. Sigler

Research output: Contribution to journalArticle

263 Citations (Scopus)

Abstract

The crystal structure of the Escherichia coli trp repressor has been solved to atomic resolution. The dimeric protein has a remarkable subunit interface in which five of each subunit's six helices are interlinked. The binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix-turn-helix motif and by moulding the details of the repressor's structure near the DNA binding surface.

Original languageEnglish (US)
Pages (from-to)782-786
Number of pages5
JournalNature
Volume317
Issue number6040
DOIs
StatePublished - 1985

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Helix-Turn-Helix Motifs
Tryptophan
Escherichia coli
DNA
Proteins
E coli TRPR protein

ASJC Scopus subject areas

  • General

Cite this

Schevitz, R. W., Otwinowski, Z., Joachimiak, A., Lawson, C. L., & Sigler, P. B. (1985). The three-dimensional structure of trp repressor. Nature, 317(6040), 782-786. https://doi.org/10.1038/317782a0

The three-dimensional structure of trp repressor. / Schevitz, Richard W.; Otwinowski, Zdzislaw; Joachimiak, Andrzej; Lawson, Catherine L.; Sigler, Paul B.

In: Nature, Vol. 317, No. 6040, 1985, p. 782-786.

Research output: Contribution to journalArticle

Schevitz, RW, Otwinowski, Z, Joachimiak, A, Lawson, CL & Sigler, PB 1985, 'The three-dimensional structure of trp repressor', Nature, vol. 317, no. 6040, pp. 782-786. https://doi.org/10.1038/317782a0
Schevitz RW, Otwinowski Z, Joachimiak A, Lawson CL, Sigler PB. The three-dimensional structure of trp repressor. Nature. 1985;317(6040):782-786. https://doi.org/10.1038/317782a0
Schevitz, Richard W. ; Otwinowski, Zdzislaw ; Joachimiak, Andrzej ; Lawson, Catherine L. ; Sigler, Paul B. / The three-dimensional structure of trp repressor. In: Nature. 1985 ; Vol. 317, No. 6040. pp. 782-786.
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