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Molten globule nature of Plasmodium falciparum P2 homo-tetramer

Pushpa Mishra1, Sinjan Choudhary2, Sujoy Mukherjee3

  • 1Department of Chemical Sciences, Tata Institute of Fundamental Research, Mumbai 400005, Maharashtra, India.

Biochemistry and Biophysics Reports
|November 11, 2017
PubMed

Insights

The Plasmodium falciparum P2 protein (PfP2) forms a dynamic tetramer at physiological pH, crucial for its non-ribosomal functions. This structure maintains molten globule characteristics, suggesting significant functional implications in the parasite.

Area of Science:

  • Structural biology
  • Parasitology
  • Biophysics

Background:

  • The P2 protein in Plasmodium falciparum exhibits a strong propensity for oligomerization, underpinning its diverse non-ribosomal functions.
  • During the parasite's nuclear division within red blood cells (RBCs), P2 translocates to the RBC surface as a tetramer.

Purpose of the Study:

  • To systematically investigate the structural dynamics and oligomerization states of the Plasmodium falciparum P2 protein (PfP2) under varying conditions.
  • To elucidate the structural basis of PfP2's function and its implications for parasite biology.

Main Methods:

  • Utilized a variety of biophysical techniques.
  • Conducted NMR spectral characteristics and relaxation dispersion measurements.
  • Analyzed protein behavior under different pH and urea concentrations.

Main Results:

  • PfP2, predominantly helical, forms a molten globule monomer at low pH.
  • At physiological pH and micromolar concentrations, PfP2 exists as a stable tetramer, formed by sideways association of two dimers with tightly packed helices.
  • The molten globule characteristics of the monomer are retained within the tetrameric structure.

Conclusions:

  • The structural dynamism of PfP2, transitioning between monomeric and tetrameric states with preserved molten globule features, is a key characteristic.
  • This inherent structural flexibility likely plays a crucial role in the transient formation of various oligomers observed in the parasite, impacting its functions.
Keywords:
Folding and dynamicsMolten globuleNMRPfP2 structurePlasmodium falciparum P2 (PfP2)

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