@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}
}
@article {49433,
	title = {Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin.},
	journal = {Nature Communications},
	volume = {9},
	year = {2018},
	month = {2018 Sep 21},
	pages = {3840},
	abstract = {<p>The bacterial type III secretion system, or injectisome, is a syringe shaped nanomachine essential for the virulence of many disease causing Gram-negative bacteria. At the core of the injectisome structure is the needle complex, a continuous channel formed by the highly oligomerized inner and outer membrane hollow rings and a polymerized helical needle filament which spans through and projects into the infected host cell. Here we present the near-atomic resolution structure of a needle complex from the prototypical Salmonella Typhimurium SPI-1 type III secretion system, with local masking protocols allowing for model building and refinement of the major membrane spanning components of the needle complex\&nbsp;base in addition to an isolated needle filament. This work provides significant insight into injectisome structure and assembly and importantly captures the molecular basis for substrate induced gating in the giant outer membrane secretin portal family.</p>
},
	issn = {2041-1723},
	doi = {10.1038/s41467-018-06298-8},
	author = {Hu, J and Worrall, L J and Hong, C and Vuckovic, M and Atkinson, C E and Caveney, N and Yu, Z and Strynadka, N C J}
}
