2W78
Structures of P. aeruginosa FpvA bound to heterologous pyoverdines: FpvA-Pvd(ATCC13535)-Fe complex
Summary for 2W78
| Entry DOI | 10.2210/pdb2w78/pdb |
| Related | 1XKH 2W16 2W6T 2W6U 2W75 2W76 2W77 |
| Descriptor | FERRIPYOVERDINE RECEPTOR, SER-LYS-GLY-FHO-LYS-FH7-SER, 3,6,9,12,15-PENTAOXATRICOSAN-1-OL, ... (6 entities in total) |
| Functional Keywords | fpva, iron, membrane, receptor, tonb box, transport, siderophore, cell membrane, ion transport, iron transport, cell outer membrane, tonb-dependent transporter |
| Biological source | PSEUDOMONAS AERUGINOSA More |
| Total number of polymer chains | 3 |
| Total formula weight | 176018.94 |
| Authors | Greenwald, J.,Nader, M.,Celia, H.,Gruffaz, C.,Meyer, J.-M.,Schalk, I.J.,Pattus, F. (deposition date: 2008-12-20, release date: 2009-05-12, Last modification date: 2023-12-13) |
| Primary citation | Greenwald, J.,Nader, M.,Celia, H.,Gruffaz, C.,Geoffroy, V.,Meyer, J.-M.,Schalk, I.J.,Pattus, F. Fpva Bound to Non-Cognate Pyoverdines: Molecular Basis of Siderophore Recognition by an Iron Transporter. Mol.Microbiol., 72:1246-, 2009 Cited by PubMed Abstract: 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. PubMed: 19504741DOI: 10.1111/J.1365-2958.2009.06721.X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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