9GTX

Structural and functional analysis of the Helicobacter pylori lipoprotein chaperone LolA

Summary for 9GTX

• Entry DOI: 10.2210/pdb9gtx/pdb
• Descriptor: Outer-membrane lipoprotein carrier protein, DI(HYDROXYETHYL)ETHER (3 entities in total)
• Functional Keywords: lipoprotein, transport, protein transport, transport protein
• Biological source: Helicobacter pylori J99
• Total number of polymer chains: 2
• Total formula weight: 39177.27

Authors

Jaiman, D.,Persson, K. (deposition date: 2024-09-18, release date: 2024-12-18, Last modification date: 2025-01-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.04 Å)