Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
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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)
  • Received : 2013.11.10
  • Accepted : 2013.12.18
  • Published : 2013.12.20
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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

References

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