The three-dimensional structure of trp repressor

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

doi:10.1038/317782a0

The three-dimensional structure of trp repressor

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

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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 language	English (US)
Pages (from-to)	782-786
Number of pages	5
Journal	Nature
Volume	317
Issue number	6040
DOIs	https://doi.org/10.1038/317782a0
State	Published - 1985

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title = "The three-dimensional structure of trp repressor",

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.",

author = "Schevitz, {Richard W.} and Zdzislaw Otwinowski and Andrzej Joachimiak and Lawson, {Catherine L.} and Sigler, {Paul B.}",

year = "1985",

doi = "10.1038/317782a0",

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T1 - The three-dimensional structure of trp repressor

AU - Schevitz, Richard W.

AU - Otwinowski, Zdzislaw

AU - Joachimiak, Andrzej

AU - Lawson, Catherine L.

AU - Sigler, Paul B.

PY - 1985

Y1 - 1985

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AB - 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.

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The three-dimensional structure of trp repressor

Abstract

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