6U2D

PmtCD peptide exporter basket domain

Summary for 6U2D

• Entry DOI: 10.2210/pdb6u2d/pdb
• Related: 6U2C
• Descriptor: ABC transporter ATP-binding protein, SULFATE ION, IODIDE ION, ... (4 entities in total)
• Functional Keywords: abc transporter, abc exporter, peptide transort, membrane protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 4
• Total formula weight: 32379.53

Authors

Zeytuni, N.,Strynadka, N.C.J. (deposition date: 2019-08-19, release date: 2020-10-14, Last modification date: 2024-03-13)

Primary citation

Zeytuni, N.,Dickey, S.W.,Hu, J.,Chou, H.T.,Worrall, L.J.,Alexander, J.A.N.,Carlson, M.L.,Nosella, M.,Duong, F.,Yu, Z.,Otto, M.,Strynadka, N.C.J.
Structural insight into the Staphylococcus aureus ATP-driven exporter of virulent peptide toxins
Sci Adv, 6:eabb8219-, 2020

PubMed Abstract: 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.

PubMed: 32998902
DOI: 10.1126/sciadv.abb8219

Experimental method

X-RAY DIFFRACTION (2.11 Å)