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-Structure paper
| タイトル | MprF from is a promiscuous lipid scramblase with broad substrate specificity. |
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| ジャーナル・号・ページ | Sci Adv, Vol. 11, Issue 15, Page eads9135, Year 2025 |
| 掲載日 | 2025年4月11日 |
著者 | Matthew T K Hankins / Matyas Parrag / Alisa A Garaeva / Jennifer C Earp / Markus A Seeger / Phillip J Stansfeld / Maike Bublitz / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Sci Adv / PubMed:40203087 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.28 Å |
| 構造データ | EMDB-51497, PDB-9goe: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / Lipid Transport / Sybody complex / Antimicrobial Resistance / Saposin-protein Nanoparticle |
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pseudomonas aeruginosa pao1 (緑膿菌)
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