Spatial arrangement of the three alpha helices in the solution conformation of E. coli lac repressor DNA-binding domain.

E.R. Zuiderweg; M. Billeter; R. Boelens; R.M. Scheek; K. Wüthrich; R. Kaptein

Spatial arrangement of the three alpha helices in the solution conformation of E. coli lac repressor DNA-binding domain.

E.R. Zuiderweg, M. Billeter, R. Boelens, R.M. Scheek, K. Wüthrich, R. Kaptein

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

Abstract

The relative orientations of the 3 helices in the DNA-binding domain ('headpiece') of lac repressor have been determined using distance constraints obtained from 2-dimensional 1H nuclear Overhauser enhancement spectra. The relative orientations of its helices is similar to that of the central 3 helices in the DNA-binding domain of the lambda repressor of the bacteriophage lambda.

Original language	English
Pages (from-to)	243-247
Number of pages	5
Journal	FEBS Letters
Volume	174
Issue number	2
Publication status	Published - 1984
Externally published	Yes

Keywords

bacterial DNA
repressor protein
transcription factor
article
Escherichia coli
metabolism
protein conformation
solution and solubility
spectroscopy

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https://febs.onlinelibrary.wiley.com/doi/abs/10.1016/0014-5793%2884%2981166-7

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title = "Spatial arrangement of the three alpha helices in the solution conformation of E. coli lac repressor DNA-binding domain.",

abstract = "The relative orientations of the 3 helices in the DNA-binding domain ('headpiece') of lac repressor have been determined using distance constraints obtained from 2-dimensional 1H nuclear Overhauser enhancement spectra. The relative orientations of its helices is similar to that of the central 3 helices in the DNA-binding domain of the lambda repressor of the bacteriophage lambda.",

keywords = "bacterial DNA, repressor protein, transcription factor, article, Escherichia coli, metabolism, protein conformation, solution and solubility, spectroscopy",

author = "E.R. Zuiderweg and M. Billeter and R. Boelens and R.M. Scheek and K. W{\"u}thrich and R. Kaptein",

year = "1984",

language = "English",

volume = "174",

pages = "243--247",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "2",

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T1 - Spatial arrangement of the three alpha helices in the solution conformation of E. coli lac repressor DNA-binding domain.

AU - Zuiderweg, E.R.

AU - Billeter, M.

AU - Boelens, R.

AU - Scheek, R.M.

AU - Wüthrich, K.

AU - Kaptein, R.

PY - 1984

Y1 - 1984

N2 - The relative orientations of the 3 helices in the DNA-binding domain ('headpiece') of lac repressor have been determined using distance constraints obtained from 2-dimensional 1H nuclear Overhauser enhancement spectra. The relative orientations of its helices is similar to that of the central 3 helices in the DNA-binding domain of the lambda repressor of the bacteriophage lambda.

AB - The relative orientations of the 3 helices in the DNA-binding domain ('headpiece') of lac repressor have been determined using distance constraints obtained from 2-dimensional 1H nuclear Overhauser enhancement spectra. The relative orientations of its helices is similar to that of the central 3 helices in the DNA-binding domain of the lambda repressor of the bacteriophage lambda.

KW - bacterial DNA

KW - repressor protein

KW - transcription factor

KW - article

KW - Escherichia coli

KW - metabolism

KW - protein conformation

KW - solution and solubility

KW - spectroscopy

M3 - Article

SN - 0014-5793

VL - 174

SP - 243

EP - 247

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Spatial arrangement of the three alpha helices in the solution conformation of E. coli lac repressor DNA-binding domain.

Abstract

Keywords

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