2w77 | pdb_00002w77

Structures of P. aeruginosa FpvA bound to heterologous pyoverdines: FpvA-Pvd(Pfl18.1)-Fe complex

spinqualitylabelsall models 2w77, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w77 is a 3 chain structure with sequence from Pseudomonas aeruginosa PAO1 and Pseudomonas fluorescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: DSN, FE, FH7, FHO, N8E, PO4, PVE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FPVA_PSEAE Receptor for the siderophore ferripyoverdine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The first step in the specific uptake of iron via siderophores in Gram-negative bacteria is the recognition and binding of a ferric siderophore by its cognate receptor. We investigated the molecular basis of this event through structural and biochemical approaches. FpvA, the pyoverdine-Fe transporter from Pseudomonas aeruginosa ATCC 15692 (PAO1 strain), is able to transport ferric-pyoverdines originating from other species, whereas most fluorescent pseudomonads are only able to use the one they produce among the more than 100 known different pyoverdines. We solved the structure of FpvA bound to non-cognate pyoverdines of high- or low-affinity and found a close correlation between receptor-ligand structure and the measured affinities. The structure of the first amino acid residues of the pyoverdine chain distinguished the high- and low-affinity binders while the C-terminal portion of the pyoverdines, often cyclic, does not appear to contribute extensively to the interaction between the siderophore and its transporter. The specificity of the ferric-pyoverdine binding site of FpvA is conferred by the structural elements common to all ferric-pyoverdines, i.e. the chromophore, iron, and its chelating groups. FpvA bound to non-cognate pyoverdines: molecular basis of siderophore recognition by an iron transporter.,Greenwald J, Nader M, Celia H, Gruffaz C, Geoffroy V, Meyer JM, Schalk IJ, Pattus F Mol Microbiol. 2009 Jun;72(5):1246-59. PMID:19504741 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferripyoverdine receptor

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