6FHM

Crystal structure of the F47E mutant of the lipoprotein localization factor, LolA

6FHM の概要

• エントリーDOI: 10.2210/pdb6fhm/pdb
• 関連するPDBエントリー: 6F3Z 6F49
• 分子名称: Outer-membrane lipoprotein carrier protein, GLYCEROL (3 entities in total)
• 機能のキーワード: lipoprotein transport, domain-swapped dimer, protein transport
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46110.58

構造登録者

Kaplan, E.,Greene, N.P.,Crow, A.,Koronakis, V. (登録日: 2018-01-15, 公開日: 2018-07-25, 最終更新日: 2024-01-17)

主引用文献

Kaplan, E.,Greene, N.P.,Crow, A.,Koronakis, V.
Insights into bacterial lipoprotein trafficking from a structure of LolA bound to the LolC periplasmic domain.
Proc. Natl. Acad. Sci. U.S.A., 115:E7389-E7397, 2018

PubMed Abstract: In Gram-negative bacteria, outer-membrane lipoproteins are essential for maintaining cellular integrity, transporting nutrients, establishing infections, and promoting the formation of biofilms. The LolCDE ABC transporter, LolA chaperone, and LolB outer-membrane receptor form an essential system for transporting newly matured lipoproteins from the outer leaflet of the cytoplasmic membrane to the innermost leaflet of the outer membrane. Here, we present a crystal structure of LolA in complex with the periplasmic domain of LolC. The structure reveals how a solvent-exposed β-hairpin loop (termed the "Hook") and trio of surface residues (the "Pad") of LolC are essential for recruiting LolA from the periplasm and priming it to receive lipoproteins. Experiments with purified LolCDE complex demonstrate that association with LolA is independent of nucleotide binding and hydrolysis, and homology models based on the MacB ABC transporter predict that LolA recruitment takes place at a periplasmic site located at least 50 Å from the inner membrane. Implications for the mechanism of lipoprotein extraction and transfer are discussed. The LolA-LolC structure provides atomic details on a key protein interaction within the Lol pathway and constitutes a vital step toward the complete molecular understanding of this important system.

PubMed: 30012603
DOI: 10.1073/pnas.1806822115

実験手法

X-RAY DIFFRACTION (2.39 Å)