5N7L

Crystal structure of the periplasmic domain of XcpY, tI crystal form.

5N7L の概要

• エントリーDOI: 10.2210/pdb5n7l/pdb
• 分子名称: Type II secretion system protein L, BROMIDE ION, GLUTAMIC ACID, ... (4 entities in total)
• 機能のキーワード: periplasm, ferrodoxin fold, gspl protein, protein transport
• 由来する生物種: Pseudomonas aeruginosa PAO1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8793.22

構造登録者

Fulara, A.,Savvides, S.N. (登録日: 2017-02-20, 公開日: 2018-03-14, 最終更新日: 2024-01-17)

主引用文献

Fulara, A.,Vandenberghe, I.,Read, R.J.,Devreese, B.,Savvides, S.N.
Structure and oligomerization of the periplasmic domain of GspL from the type II secretion system of Pseudomonas aeruginosa.
Sci Rep, 8:16760-16760, 2018

PubMed Abstract: The ability of bacteria to infect a host relies in part on the secretion of molecular virulence factors across the cell envelope. Pseudomonas aeruginosa, a ubiquitous environmental bacterium causing opportunistic infections in humans, employs the type II secretion system (T2SS) to transport effector proteins across its cellular envelope as part of a diverse array of virulence strategies. General secretory pathway protein L (GspL) is an essential inner-membrane component of the T2SS apparatus, and is thought to facilitate transduction of the energy from ATP hydrolysis in the cytoplasm to the periplasmic components of the system. However, our incomplete understanding of the assembly principles of the T2SS machinery prevents the mechanistic deconvolution of T2SS-mediated protein secretion. Here we show via two crystal structures that the periplasmic ferredoxin-like domain of GspL (GspL) is a dimer stabilized by hydrophobic interactions, and that this interface may allow significant interdomain plasticity. The general dimerization mode of GspL is shared with GspL from Vibrio parahaemolyticus suggesting a conserved oligomerization mode across the GspL family. Furthermore, we identified a tetrameric form of the complete periplasmic segment of GspL (GspL) which indicates that GspL may be able to adopt multiple oligomeric states as part of its dynamic role in the T2SS apparatus.

PubMed: 30425318
DOI: 10.1038/s41598-018-34956-w

実験手法

X-RAY DIFFRACTION (2.501 Å)