9X4A
Cryo-EM structure of Streptococcus thermophilus FoeAB E504Q mutant in complex with ATP
Summary for 9X4A
| Entry DOI | 10.2210/pdb9x4a/pdb |
| EMDB information | 66535 |
| Descriptor | Lipid/multidrug/protein-type ABC exporter, ATP binding/membrane-spanning protein, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | transport protein |
| Biological source | Streptococcus thermophilus More |
| Total number of polymer chains | 2 |
| Total formula weight | 134805.74 |
| Authors | Taguchi, A.,Fujita, J.,Namba, K.,Nishino, K. (deposition date: 2025-10-10, release date: 2026-06-03, Last modification date: 2026-09-09) |
| Primary citation | Taguchi, A.,Fujita, J.,Tanabe, M.,Takaya, D.,Harada, K.,Moriya, T.,Fukuzawa, K.,Namba, K.,Nishino, K. Structural insights into fosfomycin efflux by a streptococcal ABC transporter. Proc.Natl.Acad.Sci.USA, 123:e2535933123-e2535933123, 2026 Cited by PubMed Abstract: Gram-positive bacteria encode a broad array of ABC transporters that mediate substrate translocation across the cell membrane, with some contributing to their survival under environmental stresses such as antimicrobial exposure. While several of these transporters have been shown to exhibit multidrug efflux activity, the functional roles of many others remain unknown. Here, using an efflux pump screen in the opportunistic human pathogen , we identified a previously uncharacterized type IV ABC transporter (FoeAB) that confers resistance to the antibiotic fosfomycin. We show that purified FoeAB mediates fosfomycin transport in a liposome-reconstituted system and provide evidence that it functions as a multidrug efflux pump with substrate preferences distinct from those of known efflux pumps. Furthermore, we present cryogenic electron microscopy (cryo-EM) structures of FoeAB in inward- and outward-facing states, which reveal conformational changes associated with nucleotide binding and identify residues important for substrate transport. Collectively, these findings expand the known repertoire of antibiotic-exporting ABC transporters in Gram-positive bacteria and provide structural insight into the underlying transport mechanism. PubMed: 42664038DOI: 10.1073/pnas.2535933123 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.16 Å) |
Structure validation
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