6R1F
Crystal structure of the ferric enterobactin receptor mutant R480A from Pseudomonas aeruginosa (PfeA) in complex with enterobactin
「6I2L」から置き換えられました6R1F の概要
エントリーDOI | 10.2210/pdb6r1f/pdb |
分子名称 | Ferric enterobactin receptor, FE (III) ION, N,N',N''-[(3S,7S,11S)-2,6,10-trioxo-1,5,9-trioxacyclododecane-3,7,11-triyl]tris(2,3-dihydroxybenzamide), ... (4 entities in total) |
機能のキーワード | pfea, pa2688, outer membrane receptor, membrane protein, protochelin |
由来する生物種 | Pseudomonas aeruginosa PAO1 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 79124.40 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 31413254DOI: 10.1038/s41467-019-11508-y 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.11 Å) |
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