9GOE
Cryo-EM structure of the multiple peptide resistance factor (MprF) from Pseudomonas aeruginosa bound to a synthetic nanobody (Sb29)
9GOE の概要
エントリーDOI | 10.2210/pdb9goe/pdb |
EMDBエントリー | 51497 |
分子名称 | Phosphatidylglycerol lysyltransferase, Synthetic nanobody (Sybody) 29 (2 entities in total) |
機能のキーワード | lipid transport, sybody complex, antimicrobial resistance, saposin-protein nanoparticle, membrane protein |
由来する生物種 | Pseudomonas aeruginosa PAO1 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 112892.57 |
構造登録者 | Hankins, M.T.K.,Parrag, M.,Garaeva, A.A.,Earp, J.C.,Seeger, M.A.,Stansfeld, P.J.,Bublitz, M. (登録日: 2024-09-05, 公開日: 2025-03-12, 最終更新日: 2025-04-23) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.28 Å) |
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