3sao

The Siderocalin Ex-FABP functions through dual ligand specificities

spinqualitylabelsall models 3sao, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sao is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: DBH, FE, GOL, NKN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EXFAB_CHICK Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor. Publication Abstract from PubMed Galline Ex-FABP was identified as another candidate antibacterial, catecholate siderophore binding lipocalin (siderocalin) based on structural parallels with the family archetype, mammalian Siderocalin. Binding assays show that Ex-FABP retains iron in a siderophore-dependent manner in both hypertrophic and dedifferentiated chondrocytes, where Ex-FABP expression is induced after treatment with proinflammatory agents, and specifically binds ferric complexes of enterobactin, parabactin, bacillibactin and, unexpectedly, monoglucosylated enterobactin, which does not bind to Siderocalin. Growth arrest assays functionally confirm the bacteriostatic effect of Ex-FABP in vitro under iron-limiting conditions. The 1.8 A crystal structure of Ex-FABP explains the expanded specificity, but also surprisingly reveals an extended, multi-chambered cavity extending through the protein and encompassing two separate ligand specificities, one for bacterial siderophores (as in Siderocalin) at one end and one specifically binding copurified lysophosphatidic acid, a potent cell signaling molecule, at the other end, suggesting Ex-FABP employs dual functionalities to explain its diverse endogenous activities. Galline Ex-FABP Is an Antibacterial Siderocalin and a Lysophosphatidic Acid Sensor Functioning through Dual Ligand Specificities.,Correnti C, Clifton MC, Abergel RJ, Allred B, Hoette TM, Ruiz M, Cancedda R, Raymond KN, Descalzi F, Strong RK Structure. 2011 Dec 7;19(12):1796-806. PMID:22153502 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Siderocalin 3D structures

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