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Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
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Backbone resonance assignments of the outer membrane lipoprotein FrpD from Neisseria meningitidis

Ladislav Bumba1, Ekaterina Sviridova, Ivana Kutá Smatanová

  • 1Institute of Microbiology of the ASCR, v.v.i., Videnska 1083, Prague, 142 20, Czech Republic.

Biomolecular NMR Assignments
|December 11, 2012
PubMed

Insights

Neisseria meningitidis FrpD protein, an outer membrane lipoprotein, interacts closely with the FrpC protein. This study provides chemical shift assignments for FrpD(43-271) to understand this bacterial interaction.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • FrpD is an iron-regulated lipoprotein in the Neisseria meningitidis outer membrane.
  • Its function is unknown, but it may anchor the Type I-secreted FrpC protein to the bacterial surface.
  • FrpC belongs to the Repeat in ToXins (RTX) protein family and binds FrpD with high affinity.

Purpose of the Study:

  • To assign the backbone (1)H, (13)C, and (15)N chemical shifts for the FrpD(43-271) protein.
  • To characterize the interaction between FrpD and the N-terminal domain of FrpC.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used for chemical shift assignments.
  • Analysis of backbone (1)H, (13)C, and (15)N resonances of FrpD(43-271).

Main Results:

  • Complete backbone chemical shift assignments for FrpD(43-271) were obtained.
  • These assignments provide a foundation for characterizing the FrpD-FrpC interaction at an atomic level.

Conclusions:

  • The obtained chemical shift assignments are crucial for future structural and functional studies of the FrpD-FrpC complex.
  • Understanding this interaction could shed light on the biological role of FrpD in Neisseria meningitidis.

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