Abstract
To obtain essential metal ions, human pathogens secrete virulence-associated siderophores at first and then retake the metal-chelated siderophores through a subfamily of ATP-binding cassette (ABC) importer, however, the molecular mechanisms are completely unknown till now. Here, we have determined multiple structures of yersiniabactin importer YbtPQ complex from uropathogenic Escherichia coli (UPEC) at inward-open conformation in both apo and substrate-bound states by cryo electron microscopy. Surprisingly, YbtPQ does not adopt any known fold of ABC importers, but adopt the fold of Type IV ABC exporters.
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