9GTX

Structural and functional analysis of the Helicobacter pylori lipoprotein chaperone LolA

9GTX の概要

• エントリーDOI: 10.2210/pdb9gtx/pdb
• 分子名称: Outer-membrane lipoprotein carrier protein, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: lipoprotein, transport, protein transport, transport protein
• 由来する生物種: Helicobacter pylori J99
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39177.27

構造登録者

Jaiman, D.,Persson, K. (登録日: 2024-09-18, 公開日: 2024-12-18, 最終更新日: 2025-01-15)

主引用文献

Jaiman, D.,Persson, K.
Structural and functional analysis of the Helicobacter pylori lipoprotein chaperone LolA.
Front Microbiol, 15:1512451-1512451, 2024

PubMed Abstract: Lipoproteins are crucial for maintaining the structural integrity of bacterial membranes. In Gram-negative bacteria, the localization of lipoprotein (Lol) system facilitates the transport of these proteins from the inner membrane to the outer membrane. In , an ε-proteobacterium, lipoprotein transport differs significantly from the canonical and well-studied system in , particularly due to the absence of LolB and the use of a LolF homodimer instead of the LolCE heterodimer. This study presents the crystal structure of the lipoprotein chaperone LolA (LolA-HP) and its interaction with lipopeptide antibiotics such as polymyxin B and colistin. Isothermal titration calorimetry revealed that, unlike LolA from and , LolA-HP does not bind to these antibiotics. Structural comparisons showed that LolA-HP has a deeper hydrophobic cleft but lacks the negative electrostatic potential critical for binding polymyxins. These findings offer insights into the structural diversity of LolA across bacterial species and its potential as a target for antibacterial agents.

PubMed: 39749131
DOI: 10.3389/fmicb.2024.1512451

実験手法

X-RAY DIFFRACTION (2.04 Å)