期刊
NATURE COMMUNICATIONS
卷 10, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-11508-y
关键词
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资金
- Innovative Medicines Initiatives Joint Undertaking [115525, 115583]
- European Union
- Wellcome Trust [100209/Z/12/Z]
- MIUR [2015795S5W_005]
- Vaincre la Mucoviscidose
- Association Gregory Lemarchal, French associations against cystic fibrosis
- EFPIA companies
- Wellcome Trust [100209/Z/12/Z] Funding Source: Wellcome Trust
Bacteria use small molecules called siderophores to scavenge iron. Siderophore-Fe3+ 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.
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