Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode
| Autor: | Betina Córsico, Kate Griffiths, Alan Cooper, Andrew J. Roe, Malcolm W. Kennedy, Brian O. Smith, Mads Gabrielsen, Gisela Raquel Franchini, Alan Riboldi-Tunnicliffe, M. Florencia Rey-Burusco, Marina Ibáñez-Shimabukuro |
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| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
fatty acid binding protein nematode Biophysics As-p18 Fatty Acid-Binding Proteins Ligands Biochemistry Protein Structure Secondary Fatty acid-binding protein nemFABP purl.org/becyt/ford/1 [https] 03 medical and health sciences Protein Domains Extracellular Fatty acid binding protein Animals Parasitic helminths purl.org/becyt/ford/1.6 [https] Molecular Biology Ascaris suum Research Articles Ovum chemistry.chemical_classification 030102 biochemistry & molecular biology biology Chemistry Fatty acid Helminth Proteins Cell Biology Nuclear magnetic resonance spectroscopy biology.organism_classification Ligand (biochemistry) Cytosol 030104 developmental biology Asp-18 parasite Intracellular Research Article Protein Binding |
| Zdroj: | Bioscience Reports CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET |
| ISSN: | 1573-4935 0144-8463 |
| Popis: | Intracellular lipid-binding proteins (iLBPs) of the fatty acid-binding protein (FABP) family of animals transport, mainly fatty acids or retinoids, are confined to the cytosol and have highly similar 3D 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 β-strand barrel capped by two short α-helices, with the carboxylate head group of oleate tethered in the interior of the protein. However, As-p18 exhibits two distinctive longer loops amongst β-strands not previously seen in a FABP. One of these is adjacent to the presumed ligand entry portal, so it 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 lig- and 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. Fil: Ibáñez, Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina Fil: Rey Burusco, M. Florencia. Universidad Nacional de La Plata. Facultad de Ciencias Médicas; Argentina Fil: Gabrielsen, Mads. University of Glasgow; Reino Unido Fil: Franchini, Gisela Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina Fil: Riboldi Tunnicliffe, Alan. Australian Synchrotron; Australia Fil: Roe, Andrew J.. University of Glasgow; Reino Unido Fil: Griffiths, Kate. University of Glasgow; Reino Unido Fil: Cooper, Alan. University of Glasgow; Reino Unido Fil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina Fil: Kennedy, Malcolm W.. University of Glasgow; Reino Unido Fil: Smith, Brian O.. University of Glasgow; Reino Unido |
| Databáze: | OpenAIRE |
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