9GOE
Cryo-EM structure of the multiple peptide resistance factor (MprF) from Pseudomonas aeruginosa bound to a synthetic nanobody (Sb29)
Summary for 9GOE
| Entry DOI | 10.2210/pdb9goe/pdb |
| EMDB information | 51497 |
| Descriptor | Phosphatidylglycerol lysyltransferase, Synthetic nanobody (Sybody) 29 (2 entities in total) |
| Functional Keywords | lipid transport, sybody complex, antimicrobial resistance, saposin-protein nanoparticle, membrane protein |
| Biological source | Pseudomonas aeruginosa PAO1 More |
| Total number of polymer chains | 2 |
| Total formula weight | 112892.57 |
| Authors | Hankins, M.T.K.,Parrag, M.,Garaeva, A.A.,Earp, J.C.,Seeger, M.A.,Stansfeld, P.J.,Bublitz, M. (deposition date: 2024-09-05, release date: 2025-03-12, Last modification date: 2025-04-23) |
| Primary citation | Hankins, M.T.K.,Parrag, M.,Garaeva, A.A.,Earp, J.C.,Seeger, M.A.,Stansfeld, P.J.,Bublitz, M. MprF from Pseudomonas aeruginosa is a promiscuous lipid scramblase with broad substrate specificity. Sci Adv, 11:eads9135-eads9135, 2025 Cited by PubMed Abstract: The multiple peptide resistance factor (MprF) is a bifunctional membrane protein found in many bacteria, including and . MprF modifies inner leaflet lipid headgroups through aminoacylation and translocates modified lipid to the outer leaflet. This activity provides increased resistance to antimicrobial agents. MprF presents a promising target in multiresistant pathogens, but structural information is limited and both substrate specificity and energization of MprF-mediated lipid transport are poorly understood. Here, we present the cryo-EM structure of MprF from (MprF) bound to a synthetic nanobody. MprF adopts an "open" conformation with a wide, lipid-exposed groove on the periplasmic side that induces a local membrane deformation in molecular dynamics simulations. Using an in vitro liposome transport assay, we demonstrate that MprF translocates a wide range of different lipids without an external energy source. This suggests that MprF is the first dedicated lipid scramblase to be characterized in bacteria. PubMed: 40203087DOI: 10.1126/sciadv.ads9135 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.28 Å) |
Structure validation
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