5X5Y

A membrane protein complex

5X5Y の概要

• エントリーDOI: 10.2210/pdb5x5y/pdb
• 分子名称: Probable ATP-binding component of ABC transporter, Uncharacterized protein (3 entities in total)
• 機能のキーワード: membrane protein, transporter
• 由来する生物種: Pseudomonas aeruginosa PAO1; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 134212.67

構造登録者

Luo, Q.,Yang, X.,Huang, Y. (登録日: 2017-02-18, 公開日: 2017-04-05, 最終更新日: 2023-11-22)

主引用文献

Luo, Q.,Yang, X.,Yu, S.,Shi, H.,Wang, K.,Xiao, L.,Zhu, G.,Sun, C.,Li, T.,Li, D.,Zhang, X.,Zhou, M.,Huang, Y.
Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG
Nat. Struct. Mol. Biol., 24:469-474, 2017

PubMed Abstract: After biosynthesis, bacterial lipopolysaccharides (LPS) are transiently anchored to the outer leaflet of the inner membrane (IM). The ATP-binding cassette (ABC) transporter LptBFG extracts LPS molecules from the IM and transports them to the outer membrane. Here we report the crystal structure of nucleotide-free LptBFG from Pseudomonas aeruginosa. The structure reveals that lipopolysaccharide transport proteins LptF and LptG each contain a transmembrane domain (TMD), a periplasmic β-jellyroll-like domain and a coupling helix that interacts with LptB on the cytoplasmic side. The LptF and LptG TMDs form a large outward-facing V-shaped cavity in the IM. Mutational analyses suggest that LPS may enter the central cavity laterally, via the interface of the TMD domains of LptF and LptG, and is expelled into the β-jellyroll-like domains upon ATP binding and hydrolysis by LptB. These studies suggest a mechanism for LPS extraction by LptBFG that is distinct from those of classical ABC transporters that transport substrates across the IM.

PubMed: 28394325
DOI: 10.1038/nsmb.3399

実験手法

X-RAY DIFFRACTION (3.465 Å)