2Z4H

Crystal structure of the Cpx pathway activator NlpE from Escherichia coli

2Z4H の概要

• エントリーDOI: 10.2210/pdb2z4h/pdb
• 関連するPDBエントリー: 2Z4I
• 分子名称: Copper homeostasis protein cutF, SULFATE ION (2 entities in total)
• 機能のキーワード: outer memblane lipoprotein, beta barrel, ob-fold, 3d domain swapping, signaling protein activator
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Lipid-anchor: P40710
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51371.30

構造登録者

Hirano, Y.,Hossain, M.M.,Takeda, K.,Tokuda, H.,Miki, K. (登録日: 2007-06-18, 公開日: 2007-09-04, 最終更新日: 2024-11-06)

主引用文献

Hirano, Y.,Hossain, M.M.,Takeda, K.,Tokuda, H.,Miki, K.
Structural Studies of the Cpx Pathway Activator NlpE on the Outer Membrane of Escherichia coli
Structure, 15:963-976, 2007

PubMed Abstract: NlpE, an outer membrane lipoprotein, functions during envelope stress responses in Gram-negative bacteria. In Escherichia coli, adhesion to abiotic surfaces has been reported to activate the Cpx pathway in an NlpE-dependent manner. External copper ions are also thought to activate the Cpx pathway mediated by NlpE. We determined the crystal structure of NlpE from E. coli at 2.6 A resolution. The structure showed that NlpE consists of two beta barrel domains. The N-terminal domain resembles the bacterial lipocalin Blc, and the C-terminal domain has an oligonucleotide/oligosaccharide-binding (OB) fold. From both biochemical analyses and the crystal structure, it can be deduced that the cysteine residues in the CXXC motif may be chemically active. Furthermore, two monomers in the asymmetric unit form an unusual 3D domain-swapped dimer. These findings indicate that tertiary and/or quaternary structural instability may be responsible for Cpx pathway activation.

PubMed: 17698001
DOI: 10.1016/j.str.2007.06.014

実験手法

X-RAY DIFFRACTION (2.8 Å)