Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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Localization of the Membrane Interaction Sites of Pal-like Protein, HI0381 of Haemophilus influenzae

  • Kang, Su-Jin (Innovative Drug Research Center for Metabolic and Inflammatory Disease, Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Park, Sung Jean (Innovative Drug Research Center for Metabolic and Inflammatory Disease, Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lee, Bong-Jin (Innovative Drug Research Center for Metabolic and Inflammatory Disease, Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
  • Received : 2008.01.02
  • Accepted : 2008.03.21
  • Published : 2008.08.31
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Abstract

HI0381 of Haemophilus influenzae was investigated by circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy. HI0381 is a 153-residue peptidoglycan-associated outer membrane lipoprotein, and a part of the larger Tol/Pal network. Here, we report its backbone $^1H$, $^{15}N$, and $^{13}C$ resonance assignments, and secondary structure predictions. About 97% of all of the $^1HN$, $^{15}N$, $^{13}CO$, $^{13}C{\alpha}$, and $^{13}C{\beta}$ resonances covering 131 non-proline residues of the 134 residue, mature protein, were clarified by sequential and specific assignments. CSI and TALOS analyses revealed that HI0381 contains five ${\alpha}$-helices and five ${\beta}$-strands. To characterize the structure of HI0381, the effects of pH and salt concentration were investigated by CD. In addition, the structural changes occurring when HI0381 was in a membranous environment were investigated by comparing its HSQC spectra and CD data in buffer and in DPC micelles; the results showed that helix ${\alpha}4$ and strand ${\beta}4$ became aligned with the membrane. We conclude that the conformation of HI0381 is affected by the membrane environment, implying that its folded state is directly related to its function.

Keywords

Acknowledgement

Supported by : Korea Science Engineering Fundation

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