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JKMRS Volume 21, No 2, pp 50; Backbone NMR Assignments and Sec...
2017년 06월 20일 / 조회수: 196

Backbone NMR Assignments and Secondary Structure Determination of a Cupin-family Protein YaiE from Escherichia coli

 

 

Sung-Hee Lee1†, Dae-Won Sim1†, Eun-Hee Kim2, Ji-Hun Kim3,*, and Hyung-Sik Won1,*

 

 

1Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungbuk 27478, Korea.

2Protein Structure Group, Korea Basic Science Institute, Ochang, Chungbuk 28119, Korea

3College of Pharmacy, Chungbuk National University, Cheongju, Chungbuk 28160, Korea.

 

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 [13C/15N]-enriched sample. Subsequently, secondary structure analysis using the assigned chemical shift values identified 10 obvious β-strands and a tentative 310-helix. Taken all together, the results constitute the first structural characterization of a putative PPNP cupin protein.

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