5DL5

Crystal structure of Acinetobacter baumannii OccAB1

5DL5 の概要

• エントリーDOI: 10.2210/pdb5dl5/pdb
• 分子名称: Membrane protein, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: outer membrane protein, beta-barrel, antibiotic uptake, membrane protein
• 由来する生物種: Acinetobacter baumannii AB307-0294
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48490.33

構造登録者

Zahn, M.,Basle, A.,van den Berg, B. (登録日: 2015-09-04, 公開日: 2016-02-03, 最終更新日: 2024-01-10)

主引用文献

Zahn, M.,Bhamidimarri, S.P.,Basle, A.,Winterhalter, M.,van den Berg, B.
Structural Insights into Outer Membrane Permeability of Acinetobacter baumannii.
Structure, 24:221-231, 2016

PubMed Abstract: Bacterial resistance against antibiotics is an increasing global health problem. In Gram-negative bacteria the low permeability of the outer membrane (OM) is a major factor contributing to resistance, making it important to understand channel-mediated small-molecule passage of the OM. Acinetobacter baumannii has five Occ (OM carboxylate channel) proteins, which collectively are of major importance for the entry of small molecules. To improve our understanding of the OM permeability of A. baumannii, we present here the X-ray crystal structures of four Occ proteins, renamed OccAB1 to OccAB4. In addition we have carried out a biochemical and biophysical characterization using electrophysiology and liposome swelling experiments, providing information on substrate specificities. We identify OccAB1 as having the largest pore of the Occ proteins with corresponding high rates of small-molecule uptake, and we suggest that the future design of efficient antibiotics should focus on scaffolds that can permeate efficiently through the OccAB1 channel.

PubMed: 26805524
DOI: 10.1016/j.str.2015.12.009

実験手法

X-RAY DIFFRACTION (2.05 Å)