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Assignment of 1H, 13C, and 15N resonances of YgiT, a putative DNA interacting protein from E. coli, containing one HTH and two CxxC motifs

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Abstract

The 131 residues protein encoded by the open reading frame ygiT of E. coli contains two characteristic domains: a zinc finger protein-like structure with two CxxC motives at its N-terminus and a helix-turn-helix (HTH) motif at its C-terminus. We report the backbone and side chain 1H, 13C, and 15N resonances assignment of YgiT.

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Acknowledgements

We are grateful to Professor Arne Holmgren, Department of Medical Biochemistry and Biophysics at the Karolinska Institute for help with protein purification of YgiT, and Professor Göran Karlson from the Swedish NMR center at Göteborg University for help with the acquisition of the NMR spectra. Evangelos Papadopoulos is a recipient of a scholarship from the Greek State Scholarship Foundation (I.K.Y). This work was supported by the Swedish Research Council.

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  1. Alexios Vlamis-Gardikas

    Present address: Biomedical Research Foundation, Academy of Athens, Soranou Efessiou 4, 11527, Athens, Greece

Authors and Affiliations

  1. Department of Biochemistry and Biophysics, The Arrhenius Laboratories, Stockholm University, 10691, Stockholm, Sweden

    Evangelos Papadopoulos & Astrid Gräslund

  2. Department of Chemistry, Biochemistry and Biophysics, University of Göteborg, Medicinaregatan 9E, 413 90, Goteborg, Sweden

    Martin Billeter

  3. Department of Medical Biochemistry and Biophysics, Medical Nobel Institute for Biochemistry, Karolinska Institute, Scheelesväg 2, 17177, Stockholm, Sweden

    Alexios Vlamis-Gardikas

Authors
  1. Evangelos Papadopoulos
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  2. Martin Billeter
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  3. Astrid Gräslund
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  4. Alexios Vlamis-Gardikas
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Corresponding author

Correspondence to Astrid Gräslund.

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Papadopoulos, E., Billeter, M., Gräslund, A. et al. Assignment of 1H, 13C, and 15N resonances of YgiT, a putative DNA interacting protein from E. coli, containing one HTH and two CxxC motifs. Biomol NMR Assign 1, 217–219 (2007). https://doi.org/10.1007/s12104-007-9060-x

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  • DOI: https://doi.org/10.1007/s12104-007-9060-x

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