EMD-20640

Single-particle
8.14 Å
EMD-20640 Deposition: 26/08/2019
Map released: 14/10/2020
Last modified: 14/10/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-20640

PmtCD peptide toxin ABC exporter in nucleotide free (apo) conformation

EMD-20640

Single-particle
8.14 Å
EMD-20640 Deposition: 26/08/2019
Map released: 14/10/2020
Last modified: 14/10/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Staphylococcus aureus
Sample: PmtCD

Deposition Authors: Zeytuni N, Strynadka NCJ, Yu Z, Chou HT
Structural insight into the Staphylococcus aureus ATP-driven exporter of virulent peptide toxins
PUBMED: 32998902
DOI: doi:10.1126/sciadv.abb8219
ISSN: 2375-2548
Abstract:
Staphylococcus aureus 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'-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.