5M9B

Crystal structure of the ferric enterobactin receptor (PfeA) from Pseudomonas aeruginosa

Summary for 5M9B

• Entry DOI: 10.2210/pdb5m9b/pdb
• Descriptor: Ferric enterobactin receptor, ACETIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: pfea, pa2688, outer membrane receptor, membrane protein
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 1
• Total formula weight: 79415.10

Authors

Moynie, L.,Naismith, J.H. (deposition date: 2016-11-01, release date: 2018-02-21, Last modification date: 2024-01-17)

Primary citation

Moynie, L.,Milenkovic, S.,Mislin, G.L.A.,Gasser, V.,Malloci, G.,Baco, E.,McCaughan, R.P.,Page, M.G.P.,Schalk, I.J.,Ceccarelli, M.,Naismith, J.H.
The complex of ferric-enterobactin with its transporter from Pseudomonas aeruginosa suggests a two-site model.
Nat Commun, 10:3673-3673, 2019

PubMed Abstract: Bacteria use small molecules called siderophores to scavenge iron. Siderophore-Fe complexes are recognised by outer-membrane transporters and imported into the periplasm in a process dependent on the inner-membrane protein TonB. The siderophore enterobactin is secreted by members of the family Enterobacteriaceae, but many other bacteria including Pseudomonas species can use it. Here, we show that the Pseudomonas transporter PfeA recognises enterobactin using extracellular loops distant from the pore. The relevance of this site is supported by in vivo and in vitro analyses. We suggest there is a second binding site deeper inside the structure and propose that correlated changes in hydrogen bonds link binding-induced structural re-arrangements to the structural adjustment of the periplasmic TonB-binding motif.

PubMed: 31413254
DOI: 10.1038/s41467-019-11508-y

Experimental method

X-RAY DIFFRACTION (2.12 Å)