4uet: Difference between revisions

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'''Unreleased structure'''


The entry 4uet is ON HOLD  until sometime in the future
==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.


Authors: REY BURUSCO, M., IBANEZ SHIMABUKURO, M., GRIFFITHS, K., COOPER, A., KENNEDY, M.W., CORSICO, B., SMITH, B.O., GRIFFITHS, K.
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>


Description: 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
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Corsico, B]]
<div class="pdbe-citations 4uet" style="background-color:#fffaf0;"></div>
[[Category: Rey Burusco, M]]
 
[[Category: Smith, B.O]]
==See Also==
[[Category: Cooper, A]]
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
[[Category: Ibanez Shimabukuro, M]]
== References ==
[[Category: Kennedy, M.W]]
<references/>
[[Category: Griffiths, K]]
__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

4uet is a 1 chain structure with sequence from Necator americanus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Rey-Burusco MF, Ibanez-Shimabukuro M, Gabrielsen M, Franchini GR, Roe AJ, Griffiths K, Zhan B, Cooper A, Kennedy MW, Corsico B, Smith BO. Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus. Biochem J. 2015 Nov 1;471(3):403-14. doi: 10.1042/BJ20150068. Epub 2015 Aug 28. PMID:26318523 doi:http://dx.doi.org/10.1042/BJ20150068
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