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PDBsum entry 4xcp
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Retinol-binding protein
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PDB id
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4xcp
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References listed in PDB file
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Key reference
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Title
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Diversity in the structures and ligand-Binding sites of nematode fatty acid and retinol-Binding proteins revealed by na-Far-1 from necator americanus.
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Authors
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M.F.Rey-Burusco,
M.Ibáñez-Shimabukuro,
M.Gabrielsen,
G.R.Franchini,
A.J.Roe,
K.Griffiths,
B.Zhan,
A.Cooper,
M.W.Kennedy,
B.Córsico,
B.O.Smith.
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Ref.
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Biochem J, 2015,
471,
403-414.
[DOI no: ]
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PubMed id
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Abstract
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Fatty acid and retinol-binding proteins (FARs) comprise a family of unusual
α-helix rich lipid-binding proteins found exclusively in nematodes. They are
secreted into host tissues by parasites of plants, animals and humans. The
structure of a FAR protein from the free-living nematode Caenorhabditis elegans
is available, but this protein [C. elegans FAR-7 (Ce-FAR-7)] is from a subfamily
of FARs that does not appear to be important at the host/parasite interface. We
have therefore examined [Necator americanus FAR-1 (Na-FAR-1)] from the
blood-feeding intestinal parasite of humans, N. americanus. The 3D structure of
Na-FAR-1 in its ligand-free and ligand-bound forms, determined by NMR (nuclear
magnetic resonance) spectroscopy and X-ray crystallography respectively, reveals
an α-helical fold similar to Ce-FAR-7, but Na-FAR-1 possesses a larger and more
complex internal ligand-binding cavity and an additional C-terminal α-helix.
Titration of apo-Na-FAR-1 with oleic acid, analysed by NMR chemical shift
perturbation, reveals that at least four distinct protein-ligand complexes can
be formed. Na-FAR-1 and possibly other FARs may have a wider repertoire for
hydrophobic ligand binding, as confirmed in the present study by our finding
that a range of neutral and polar lipids co-purify with the bacterially
expressed recombinant protein. Finally, we show by immunohistochemistry that
Na-FAR-1 is present in adult worms with a tissue distribution indicative of
possible roles in nutrient acquisition by the parasite and in reproduction in
the male.
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