4uet: Difference between revisions
New page: '''Unreleased structure''' The entry 4uet is ON HOLD until sometime in the future Authors: REY BURUSCO, M., IBANEZ SHIMABUKURO, M., GRIFFITHS, K., COOPER, A., KENNEDY, M.W., CORSICO, B.... |
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The | ==Diversity in the structures and ligand binding sites among the fatty acid and retinol binding proteins of nematodes revealed by Na-FAR-1 from Necator americanus== | ||
<StructureSection load='4uet' size='340' side='right'caption='[[4uet]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4uet]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Necator_americanus Necator americanus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UET FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uet OCA], [https://pdbe.org/4uet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uet RCSB], [https://www.ebi.ac.uk/pdbsum/4uet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uet ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/W2SRJ3_NECAM W2SRJ3_NECAM] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:26318523</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4uet" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Necator americanus]] | |||
[[Category: Cooper A]] | |||
[[Category: Corsico B]] | |||
[[Category: Griffiths K]] | |||
[[Category: Ibanez Shimabukuro M]] | |||
[[Category: Kennedy MW]] | |||
[[Category: Rey-Burusco MF]] | |||
[[Category: Smith BO]] | |||
Latest revision as of 11:20, 22 March 2023
Diversity in the structures and ligand binding sites among the fatty acid and retinol binding proteins of nematodes revealed by Na-FAR-1 from Necator americanusDiversity in the structures and ligand binding sites among the fatty acid and retinol binding proteins of nematodes revealed by Na-FAR-1 from Necator americanus
Structural highlights
FunctionPublication Abstract from PubMedFatty 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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