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, M.F., Ibañez-Shimabukuro, M., Cooper, A., Kennedy, M. W., Córsico, B. and Smith, B. O. (2014) 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. Biomolecular NMR Assignments, 8(1), pp. 19-21. (doi:10.1007/s12104-012-9444-4)

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Abstract

The fatty acid and retinol-binding (FAR) proteins are a family of unusual helix-rich lipid binding proteins found exclusively in nematodes, and are secreted by a range of parasites of humans, animals and plants. Na-FAR-1 is from the parasitic nematode Necator americanus, an intestinal blood-feeding parasite of humans. Sequence-specific 1H, 13C and 15N resonance assignments have been obtained for the recombinant 170 amino acid protein, using three-dimensional triple-resonance heteronuclear magnetic resonance experiments. Backbone assignments have been obtained for 99.3 % of the non-proline HN/N pairs (146 out of 147). The amide 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 Hα(166), Hβ(250) and Hγ(160) and 98.4 % of the Hδ (126 out of 128) atoms were assigned. In addition, 99.4 % Cα (154 out of 155) and 99.3 % Cβ (143 out of 144) resonances have been assigned. No resonances were observed for the NHn groups of R93 NεHε, arginine, Nη1H2, Nη2H2, histidine Nδ1Hδ1, Nε1Hε1 and lysine Nζ3H3. Na-FAR-1 has a similar overall arrangement of α-helices to Ce-FAR-7 of the free-living Caeorhabditis elegans, but with an extra C-terminal helix.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Kennedy, Professor Malcolm and Smith, Dr Brian and Cooper, Professor Alan
Authors: Rey-Burusco, M.F., Ibañez-Shimabukuro, M., Cooper, A., Kennedy, M. W., Córsico, B., and Smith, B. O.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
College of Medical Veterinary and Life Sciences > School of Life Sciences
College of Science and Engineering > School of Chemistry
Journal Name:Biomolecular NMR Assignments
Publisher:Springer Netherlands
ISSN:1874-2718
ISSN (Online):1874-270X
Copyright Holders:Copyright © 2012 The Authors
First Published:First published in Biomolecular NMR Assignments 8(1):19-21
Publisher Policy:Reproduced under a Creative Commons License
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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
465741Structural and biophysical analysis of novel lipid binding proteins from parasitic helminthsMalcolm KennedyWellcome Trust (WELLCOME)083625/Z/07/ZLS - ANIMAL BIOLOGY