6IC4

Cryo-EM structure of the A. baumannii MLA complex at 8.7 A resolution

6IC4 の概要

• エントリーDOI: 10.2210/pdb6ic4/pdb
• EMDBエントリー: 0007
• 分子名称: Toluene tolerance efflux transporter (ABC superfamily, PerI-bind), ABC transporter permease, ABC transporter ATP-binding protein, ... (4 entities in total)
• 機能のキーワード: membrane protein antibiotic resistance abc transporter, protein transport
• 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: 246316.62

構造登録者

Bergeron, J.R.,Kollman, J.M. (登録日: 2018-12-02, 公開日: 2019-01-23, 最終更新日: 2024-05-15)

主引用文献

Kamischke, C.,Fan, J.,Bergeron, J.,Kulasekara, H.D.,Dalebroux, Z.D.,Burrell, A.,Kollman, J.M.,Miller, S.I.
The Acinetobacter baumannii Mla system and glycerophospholipid transport to the outer membrane.
Elife, 8:-, 2019

PubMed Abstract: The outer membrane (OM) of Gram-negative bacteria serves as a selective permeability barrier that allows entry of essential nutrients while excluding toxic compounds, including antibiotics. The OM is asymmetric and contains an outer leaflet of lipopolysaccharides (LPS) or lipooligosaccharides (LOS) and an inner leaflet of glycerophospholipids (GPL). We screened transposon mutants and identified a number of mutants with OM defects, including an ABC transporter system homologous to the Mla system in We further show that this opportunistic, antibiotic-resistant pathogen uses this multicomponent protein complex and ATP hydrolysis at the inner membrane to promote GPL export to the OM. The broad conservation of the Mla system in Gram-negative bacteria suggests the system may play a conserved role in OM biogenesis. The importance of the Mla system to OM integrity and antibiotic sensitivity suggests that its components may serve as new antimicrobial therapeutic targets.

PubMed: 30638443
DOI: 10.7554/eLife.40171

実験手法

ELECTRON MICROSCOPY (8.7 Å)