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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
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Schistosoma mansoni fatty acid binding protein: specificity and functional control as revealed by crystallographic

Francesco Angelucci1, Kenneth A Johnson, Paola Baiocco

  • 1Department of Biochemical Sciences A. Rossi Fanelli, CNR Institute of Molecular Biology and Pathology and Istituto Pasteur-Fondazione Cenci Bolognetti, University of Rome La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy.

Biochemistry
|October 13, 2004
PubMed

Insights

Schistosoma mansoni fatty acid binding protein (Sm14) binds oleic acid and arachidonic acid. Structural analysis reveals Sm14

Area of Science:

  • Parasitology
  • Structural Biology
  • Biochemistry

Background:

  • Schistosomiasis is a major human parasitic disease.
  • Schistosoma mansoni relies on host fatty acids.
  • Arachidonic acid is crucial for parasite immune evasion.

Purpose of the Study:

  • Determine the structure of Sm14 bound to oleic acid and arachidonic acid.
  • Investigate Sm14's fatty acid binding site and affinity.
  • Explore the functional and physiological relevance of Sm14-fatty acid interactions.

Main Methods:

  • X-ray crystallography at 1.85 and 2.4 A resolution.
  • Fatty acid binding affinity measurements using ANS displacement.
  • Stopped-flow kinetics to determine binding/dissociation rates.

Main Results:

  • Sm14 structure with bound oleic acid and arachidonic acid elucidated.
  • Arachidonic acid shows specific interactions, including a pi-cation bond.
  • Sm14 binding site appears optimized for arachidonic acid.
  • OLA and ACD exhibit highest binding affinities.
  • Ligand binding rates are influenced by a pH-dependent conformational change.

Conclusions:

  • Structural insights into Sm14-fatty acid interactions.
  • Sm14's binding site is tailored for arachidonic acid, vital for parasite survival.
  • A pH-dependent conformational change regulates ligand binding, suggesting physiological importance.

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