@article {65759,
	title = {Structural insight into the  ATP-driven exporter of virulent peptide toxins.},
	journal = {Science Advances},
	volume = {6},
	year = {2020},
	month = {2020 Sep 30},
	abstract = {<p>is a major human pathogen that has acquired alarming broad-spectrum antibiotic resistance. One group of secreted toxins with key roles during infection is the phenol-soluble modulins (PSMs). PSMs are amphipathic, membrane-destructive cytolytic peptides that are exported to the host-cell environment by a designated adenosine 5{\textquoteright}-triphosphate (ATP)-binding cassette (ABC) transporter, the PSM transporter (PmtABCD). Here, we demonstrate that the minimal Pmt unit necessary for PSM export is PmtCD and provide its first atomic characterization by single-particle cryo-EM and x-ray crystallography. We have captured the transporter in the ATP-bound state at near atomic resolution, revealing a type II ABC exporter fold, with an additional cytosolic domain. Comparison to a lower-resolution nucleotide-free map displaying an "open" conformation and putative hydrophobic inner chamber of a size able to accommodate the binding of two PSM peptides provides mechanistic insight and sets the foundation for therapeutic design.</p>
},
	issn = {2375-2548},
	doi = {10.1126/sciadv.abb8219},
	author = {Zeytuni, N and Dickey, S W and Hu, J and Chou, H T and Worrall, L J and Alexander, J A N and Carlson, M L and Nosella, M and Duong, F and Yu, Z and Otto, M and Strynadka, N C J}
}
