6XJH
PmtCD ABC exporter without the basket domain at C2 symmetry
Summary for 6XJH
| Entry DOI | 10.2210/pdb6xjh/pdb |
| Related | 6U2D 6XFU |
| EMDB information | 20640 22194 22210 |
| Descriptor | Phenol-soluble modulin export ABC transporter permease subunit PmtD, ABC transporter ATP-binding protein, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | abc transporter, abc exporter, peptide transort, membrane protein |
| Biological source | Staphylococcus aureus More |
| Total number of polymer chains | 4 |
| Total formula weight | 128074.06 |
| Authors | Zeytuni, N.,Strynadka, N.J.C.,Hu, J.,Worrall, L.J.,Chou, H.,Yu, Z. (deposition date: 2020-06-23, release date: 2020-10-14, Last modification date: 2025-05-14) |
| 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 Cited by 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: 32998902DOI: 10.1126/sciadv.abb8219 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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