6i9f | pdb_00006i9f

Solution structure of As-p18 reveals that nematode fatty acid binding proteins exhibit unusual structural features

spinqualitylabelsall models 6i9f Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6i9f is a 1 chain structure with sequence from Ascaris suum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: OLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FABH_ASCSU Publication Abstract from PubMed Intracellular lipid binding proteins (iLBPs) of the FABP family of animals transport mainly fatty acids or retinoids, are confined to the cytosol, and have highly similar three-dimensional structures. In contrast, nematodes possess fatty acid binding proteins (nemFABPs) that are secreted into the perivitelline fluid surrounding their developing embryos. We report structures of As-p18, a nemFABP of the large intestinal roundworm Ascaris suum, with ligand bound, determined using X-ray crystallography and nuclear magnetic resonance spectroscopy. In common with other FABPs, As-p18 comprises a ten beta-strand barrel capped by two short alpha-helices, with the carboxylate head group of oleate tethered in the interior of the protein. However, As-p18 exhibits two distinctive longer loops between beta-strands not previously seen in a FABP. One of these is adjacent to the presumed ligand entry portal, so may help to target the protein for efficient loading or unloading of ligand. The second, larger loop is at the opposite end of the molecule and has no equivalent in any iLBP structure yet determined. As-p18 preferentially binds a single 18-carbon fatty acid ligand in its central cavity but in an orientation that differs from iLBPs. The unusual structural features of nemFABPs may relate to resourcing of developing embryos of nematodes. As-p18, an extracellular fatty acid binding protein of nematodes, exhibits unusual structural features.,Ibanez-Shimabukuro M, Rey-Burusco MF, Gabrielsen M, Franchini GR, Riboldi-Tunnicliffe A, Roe AJ, Griffiths K, Cooper A, Corsico B, Kennedy MW, Smith BO Biosci Rep. 2019 Jul 4. pii: BSR20191292. doi: 10.1042/BSR20191292. PMID:31273060 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fatty acid-binding protein 3D structures

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