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Acta Crystallographica Section F: Structural Biology and Crystallization Communications (1)
Biochimica et biophysica acta (1)
Córsico, Betina (2)
Cooper, Alan (1)
Falomir-Lockhart, Lisandro J. (1)
Franchini, Gisela R. (1)
Gabrielsen, Mads (1)
Griffiths, Kate (1)
Guerbi, María Ximena (1)
Ibáñez-Shimabukuro, Marina (1)
Kennedy, Malcolm W. (1)
Riboldi-Tunnicliffe, Alan (1)
Roe, Andrew J. (1)
Smith, Brian O. (1)
Storch, Judith (1)
Year of Publication
Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline
Roe, Andrew J.
Smith, Brian O.
Kennedy, Malcolm W.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
As-p18, an unusual fatty-acid-binding protein from a parasitic nematode, was expressed in bacteria, purified and crystallized. The use of a microfocus beamline was essential for data collection.
As-p18 is a fatty-acid-binding protein from the parasitic nematode Ascaris suum. Although it exhibits sequence similarity to mammalian intracellular fatty-acid-binding proteins, it contains features that are unique to nematodes. Crystals were obtained, but initial diffraction data analysis revealed that they were composed of a number of ‘microdomains’. Interpretable data could only be collected using a microfocus beamline with a beam size of 12 × 8 µm.
fatty-acid-binding proteins; parasitic nematodes; Ascaris suum; microfocus beamlines
Interaction of Enterocyte FABPs with Phospholipid Membranes: Clues for Specific Physiological Roles
Falomir-Lockhart, Lisandro J.
Franchini, Gisela R.
Guerbi, María Ximena
Biochimica et biophysica acta
Intestinal and liver fatty acid binding proteins (IFABP and LFABP, respectively), are cytosolic soluble proteins with the capacity to bind and transport hydrophobic ligands between different sub-cellular compartments. Their functions are still not clear but they are supposed to be involved in lipid trafficking and metabolism, cell growth, and regulation of several other processes, like cell differentiation. Here we investigated the interaction of these proteins with different models of phospholipid membrane vesicles in order to achieve further insight into their specificity within the enterocyte. A combination of biophysical and biochemical techniques allowed us to determine affinities of these proteins to membranes, the way phospholipid composition and vesicle size and curvature modulate such interaction, as well as the effect of protein binding on the integrity of the membrane structure. We demonstrate here that, beside their apparently opposite ligand transfer mechanisms, both LFABP and IFABP are able to interact with phospholipid membranes, but the factors that modulate such interactions are different for each protein, further implying different roles for IFABP and LFABP in the intracellular context. These results contribute to the proposed central role of intestinal FABPs in the lipid traffic within enterocytes as well as in the regulation of more complex cellular processes.
Fatty Acid Binding Proteins; Membrane Interaction; Intracellular Fatty Acid Traffic; Model Membranes
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