6Z8A
Outer membrane FoxA in complex with nocardamine
Summary for 6Z8A
| Entry DOI | 10.2210/pdb6z8a/pdb |
| Descriptor | Ferrioxamine receptor FoxA, SULFATE ION, DIMETHYL SULFOXIDE, ... (6 entities in total) |
| Functional Keywords | tonb-dependent transporter outer membrane transporter siderophore uptake transporter, membrane protein |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Total number of polymer chains | 1 |
| Total formula weight | 86606.85 |
| Authors | |
| Primary citation | Normant, V.,Josts, I.,Kuhn, L.,Perraud, Q.,Fritsch, S.,Hammann, P.,Mislin, G.L.A.,Tidow, H.,Schalk, I.J. Nocardamine-Dependent Iron Uptake in Pseudomonas aeruginosa : Exclusive Involvement of the FoxA Outer Membrane Transporter. Acs Chem.Biol., 15:2741-2751, 2020 Cited by PubMed Abstract: Iron is a key nutrient for almost all living organisms. Paradoxically, it is poorly soluble and consequently poorly bioavailable. Bacteria have thus developed multiple strategies to access this metal. One of the most common consists of the use of siderophores, small compounds that chelate ferric iron with very high affinity. Many bacteria are able to produce their own siderophores or use those produced by other microorganisms (exosiderophores) in a piracy strategy. produces two siderophores, pyoverdine and pyochelin, and is also able to use a large panel of exosiderophores. We investigated the ability of to use nocardamine (NOCA) and ferrioxamine B (DFOB) as exosiderophores under iron-limited planktonic growth conditions. Proteomic and RT-qPCR approaches showed induction of the transcription and expression of the outer membrane transporter FoxA in the presence of NOCA or DFOB in the bacterial environment. Expression of the proteins of the heme- or pyoverdine- and pyochelin-dependent iron uptake pathways was not affected by the presence of these two tris-hydroxamate siderophores. Fe uptake assays using mutants showed ferri-NOCA to be exclusively transported by FoxA, whereas ferri-DFOB was transported by FoxA and at least one other unidentified transporter. The crystal structure of FoxA complexed with NOCA-Fe revealed very similar siderophore binding sites between NOCA-Fe and DFOB-Fe. We discuss iron uptake by hydroxamate exosiderophores in cells in light of these results. PubMed: 32902248DOI: 10.1021/acschembio.0c00535 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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