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-Structure paper
タイトル | Structure and lipid dynamics in the maintenance of lipid asymmetry inner membrane complex of A. baumannii. |
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ジャーナル・号・ページ | Commun Biol, Vol. 4, Issue 1, Page 817, Year 2021 |
掲載日 | 2021年6月29日 |
著者 | Daniel Mann / Junping Fan / Kamolrat Somboon / Daniel P Farrell / Andrew Muenks / Svetomir B Tzokov / Frank DiMaio / Syma Khalid / Samuel I Miller / Julien R C Bergeron / |
PubMed 要旨 | Multi-resistant bacteria are a major threat in modern medicine. The gram-negative coccobacillus Acinetobacter baumannii currently leads the WHO list of pathogens in critical need for new therapeutic ...Multi-resistant bacteria are a major threat in modern medicine. The gram-negative coccobacillus Acinetobacter baumannii currently leads the WHO list of pathogens in critical need for new therapeutic development. The maintenance of lipid asymmetry (MLA) protein complex is one of the core machineries that transport lipids from/to the outer membrane in gram-negative bacteria. It also contributes to broad-range antibiotic resistance in several pathogens, most prominently in A. baumannii. Nonetheless, the molecular details of its role in lipid transport has remained largely elusive. Here, we report the cryo-EM maps of the core MLA complex, MlaBDEF, from the pathogen A. baumannii, in the apo-, ATP- and ADP-bound states, revealing multiple lipid binding sites in the cytosolic and periplasmic side of the complex. Molecular dynamics simulations suggest their potential trajectory across the membrane. Collectively with the recently-reported structures of the E. coli orthologue, this data also allows us to propose a molecular mechanism of lipid transport by the MLA system. |
リンク | Commun Biol / PubMed:34188171 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.9 - 4.43 Å |
構造データ | EMDB-11082, PDB-6z5u: EMDB-11083: EMDB-11084: EMDB-14398: Cryo-EM structure of the A. baumannii MlaBDEF complex bound to APPNHP |
化合物 | ChemComp-ANP: ChemComp-MG: |
由来 |
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キーワード | MEMBRANE PROTEIN / lipid transport / antibiotic resistance / ABC transporter |