4xcp

Fatty Acid and Retinol binding protein Na-FAR-1 from Necator americanus

spinqualitylabelsall models 4xcp, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xcp is a 1 chain structure with sequence from Necator americanus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.14Å Ligands: MSE, PLM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W2SRJ3_NECAM Publication Abstract from PubMed Fatty acid and retinol-binding proteins (FARs) comprise a family of unusual alpha-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 alpha-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 alpha-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. Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus.,Rey-Burusco MF, Ibanez-Shimabukuro M, Gabrielsen M, Franchini GR, Roe AJ, Griffiths K, Zhan B, Cooper A, Kennedy MW, Corsico B, Smith BO Biochem J. 2015 Nov 1;471(3):403-14. doi: 10.1042/BJ20150068. Epub 2015 Aug 28. PMID:26318523 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Retinol-binding protein 3D structures

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