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http://dx.doi.org/10.6564/JKMRS.2013.17.2.105

Backbone 1H, 15N, and 13C resonance assignments and secondary structure prediction of NifU-like protein, HP1492 from Helicobacter Pylori  

Lee, Ki-Young (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
Kang, Su-Jin (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
Bae, Ye-Ji (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
Lee, Kyu-Yeon (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
Kim, Ji-Hun (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
Lee, Ingyun (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
Lee, Bong-Jin (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
Publication Information
Journal of the Korean Magnetic Resonance Society / v.17, no.2, 2013 , pp. 105-110 More about this Journal
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 ${\alpha}$-helices and three ${\beta}$-sheets. This study is an essential step towards the structural characterization of HP1492.
Keywords
Helicobacter pylori; NifU-like protein; HP1492; NMR;
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