9WMI
PsdAB dimer(LMNG)
Summary for 9WMI
| Entry DOI | 10.2210/pdb9wmi/pdb |
| EMDB information | 66092 |
| Descriptor | Lantibiotic ABC transporter ATP-binding protein PsdA, Lantibiotic ABC transporter permease PsdB, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | abc transpoter, transport protein |
| Biological source | Bacillus sp. TSA-4 More |
| Total number of polymer chains | 6 |
| Total formula weight | 265181.45 |
| Authors | |
| Primary citation | He, Y.,Fan, W.,Shi, J.,Gan, B.K.,Shao, K.,Zhu, F.,Hong, X.,Luo, M. Cryo-EM structure of the Nisin resistance pump PsdAB reveals an unusual ABC transporter architecture. Structure, 34:311-321.e5, 2026 Cited by PubMed Abstract: Bacteria have evolved diverse strategies to resist antimicrobial peptides, among them lipid II-targeting lantibiotics such as nisin. PsdAB, an ABC-type transporter regulated by the PsdRS two-component system, contributes to nisin resistance, though its structural and mechanistic basis have remained unclear. Here, we report the cryo-EM structure of Bacillus subtilis PsdAB, revealing a dimeric assembly with an unusually large central cavity at the TMD interface. Cross-linking studies confirm the dimeric nature of PsdAB both in vitro and in cells. Functional assays demonstrate that dimer-disrupting mutations compromise nisin resistance, highlighting the importance of dimerization for activity. Compared to canonical ABC transporter types, PsdAB adopts an atypical architecture comprising four NBDs and two TMDs arranged around a central cavity, which may accommodate lipid II. We propose that PsdAB represents a previously unrecognized ABC transporter class. These findings offer new insights into transporter-mediated lantibiotic resistance and suggest a potential mechanism of lipid II shielding. PubMed: 41418778DOI: 10.1016/j.str.2025.11.013 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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