The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity

R. G. Zhang; A. Joachimiak; C. L. Lawson; R. W. Schevitz; Z. Otwinowski; P. B. Sigler

doi:10.1038/327591a0

The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity

R. G. Zhang, A. Joachimiak, C. L. Lawson, R. W. Schevitz, Z. Otwinowski, P. B. Sigler

Research output: Contribution to journal › Article › peer-review

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Abstract

Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs. These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking α-helices from both subunits.

Original language	English (US)
Pages (from-to)	591-597
Number of pages	7
Journal	Nature
Volume	327
Issue number	6123
DOIs	https://doi.org/10.1038/327591a0
State	Published - 1987

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title = "The crystal structure of trp aporepressor at 1.8 {\AA} shows how binding tryptophan enhances DNA affinity",

abstract = "Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs. These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking α-helices from both subunits.",

author = "Zhang, {R. G.} and A. Joachimiak and Lawson, {C. L.} and Schevitz, {R. W.} and Z. Otwinowski and Sigler, {P. B.}",

year = "1987",

doi = "10.1038/327591a0",

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AU - Zhang, R. G.

AU - Joachimiak, A.

AU - Lawson, C. L.

AU - Schevitz, R. W.

AU - Otwinowski, Z.

AU - Sigler, P. B.

PY - 1987

Y1 - 1987

N2 - Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs. These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking α-helices from both subunits.

AB - Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs. These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking α-helices from both subunits.

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The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity

Abstract

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