6Z5U

Cryo-EM structure of the A. baumannii MlaBDEF complex bound to APPNHP

6Z5U の概要

• エントリーDOI: 10.2210/pdb6z5u/pdb
• EMDBエントリー: 11082
• 分子名称: ABC transporter permease, Anti-sigma factor antagonist, MCE family protein, ... (6 entities in total)
• 機能のキーワード: lipid transport, antibiotic resistance, abc transporter, membrane protein
• 由来する生物種: Acinetobacter baumannii; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 283002.86

構造登録者

Mann, D.,Bergeron, J.R.C. (登録日: 2020-05-27, 公開日: 2021-05-05, 最終更新日: 2024-05-22)

主引用文献

Mann, D.,Fan, J.,Somboon, K.,Farrell, D.P.,Muenks, A.,Tzokov, S.B.,DiMaio, F.,Khalid, S.,Miller, S.I.,Bergeron, J.R.C.
Structure and lipid dynamics in the maintenance of lipid asymmetry inner membrane complex of A. baumannii.
Commun Biol, 4:817-817, 2021

PubMed Abstract: 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.

PubMed: 34188171
DOI: 10.1038/s42003-021-02318-4

実験手法

ELECTRON MICROSCOPY (3.9 Å)