1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus.

REY-BURUSCO, FLORENCIA; IBAÑEZ-SHIMABUKURO , MARINA; COOPER A; KENNEDY MW; CÓRSICO, B; SMITH BO

BIOMOLECULAR NMR ASSIGNMENTS

SPRINGER

Lugar: Berlin; Año: 2012

1874-2718

The fatty acid and retinol-binding (FAR) proteins are a family of unusual helix-rich lipidbinding proteins found exclusively in nematodes, and are secreted by a range of parasites ofhumans, animals and plants. Na-FAR-1 is from the parasitic nematode Necator americanus, anintestinal blood-feeding parasite of humans. Sequence-specific 1H, 13C and 15N resonanceassignments have been obtained for the recombinant 170 amino acid protein, using threedimensionaltriple-resonance heteronuclear magnetic resonance experiments. Backboneassignments have been obtained for 99.3% of the non-proline HN/N pairs (146 out of 147). Theamide resonance of T45 was not observed, probably due to rapid exchange with solvent water.A total of 96.9% of backbone resonances were identified, while 97.7% assignment of amino acid sidechain protons is complete. All Ha(166), Hβ(250) and Hg(160) and 98.4% of the Hd(126 out of 128) atoms were assigned. In addition, 99.4% Ca (154 out of 155) and 99.3% Cβ(143 out of 144) resonances have been assigned. No resonances were observed for the NHngroups of R93 NeHe, arginine, Nn11H2, Nn2H2, histidine Nd1Hd1, Ne1He1 and lysine Ns3H3. Na-FAR-1 has a similar overall arrangement of a-helices to Ce-FAR-7 of the free-livingCaeorhabditis elegans, but with an extra C-terminal helix