Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
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Backbone NMR Assignments and Secondary Structure Determination of a Cupin-family Protein YaiE from Escherichia coli

  • Lee, Sung-Hee (Department of Biotechnology, College of Biomedical and Health Science, Konkuk University) ;
  • Sim, Dae-Won (Department of Biotechnology, College of Biomedical and Health Science, Konkuk University) ;
  • Kim, Eun-Hee (Protein Structure Group, Korea Basic Science Institute) ;
  • Kim, Ji-Hun (College of Pharmacy, Chungbuk National University) ;
  • Won, Hyung-Sik (Department of Biotechnology, College of Biomedical and Health Science, Konkuk University)
  • Received : 2017.04.02
  • Accepted : 2017.04.29
  • Published : 2017.06.20
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Abstract

Cupin-superfamily proteins represent the most functionally diverse groups of proteins and include a huge number of functionally uncharacterized proteins. Recently, YaiE, a cupin protein from Escherichia coli has been suggested to be involved in a novel activity of pyrimidine/purine nucleoside phosphorylase (PPNP). In the present study, we achieved a complete backbone NMR assignments of YaiE, by a series of heteronuclear multidimensional NMR experiments on its [$^{13}C/^{15}N$]-enriched sample. Subsequently, secondary structure analysis using the assigned chemical shift values identified 10 obvious ${\beta}-strands$ and a tentative $3_{10}-helix$. Taken all together, the results constitute the first structural characterization of a putative PPNP cupin protein.

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