투고논문
| JKMRS Volume 17, No. 2, 105-110 : Backbone 1H, 15N, and 13C re... | |
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| 2013년 12월 20일 / 조회수: 845 | |
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Backbone 1H, 15N, and 13C resonance assignments and secondary structure prediction of NifU-like protein, HP1492 from Helicobacter Pylori Ki-Young Lee1†, Su-Jin Kang1†, Ye-Ji Bae1, Kyu-Yeon Lee1, Ji-Hun Kim1, Ingyun Lee1 and Bong-Jin Lee1* 1Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, San 56-1, Shillim-Dong, Kwanak-Gu, Received Nov 10, 2013; Revised Dec 09, 2013; Accepted Dec 18, 2013 Abstract HP1492 is a NifU-like protein of Helicobacter pylori (H. pylori) and plays a role as a scaffold which transfer Fe-S cluster to Fe-S proteins like Ferredoxin. To understand how to bind to iron ion or iron-sulfur cluster, HP1492 was expressed and purified in Escherichia coli (E. coli). From the NMR measurement, we could carry out the sequence specific backbone resonance assignment of HP1492. Approximately 91% of all resonances could be assigned unambiguously. By analyzing results of CSI and TALOS from NMR data, we could predict the secondary structure of HP1492, which consists of three a-helices and three b-sheets. This study is an essential step towards the structural characterization of HP1492. |
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| 첨부파일 | 7이봉진.pdf |