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Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state

2014; National Academy of Sciences; Volume: 111; Issue: 25 Linguagem: Inglês

10.1073/pnas.1320506111

1091-6490

Hassanul G. Choudhury, Zhen Tong, Indran Mathavan, Yanyan Li, So Iwata, Séverine Zirah, Sylvie Rebuffat, Hendrik W. van Veen, Konstantinos Beis,

Antimicrobial Peptides and Activities

Significance ATP-binding cassette (ABC) exporters transport substrates by an alternating access mechanism that is driven by ATP binding and hydrolysis. The general mechanism is a motion from an inward to an outward state, with a different intertwining of the half-transporters in both states. In this study we determined the function and crystal structure of the ABC exporter McjD that exports the antibacterial peptide microcin J25. Our structure represents a novel nucleotide-bound, outward-occluded state. It does not possess subunit intertwining and shows a well-defined binding cavity that is closed to all sides, consistent with it being an intermediate between the inward- and outward-facing state. Our structure provides valuable insights in a transition state of an ABC exporter.