2D1U

Solution structure of the periplasmic signaling domain of FecA from Escherichia coli

2D1U の概要

• エントリーDOI: 10.2210/pdb2d1u/pdb
• NMR情報: BMRB: 6803
• 分子名称: Iron(III) dicitrate transport protein fecA (1 entity in total)
• 機能のキーワード: feca, surface signaling, iron-uptake, metal transport
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11152.09

構造登録者

Garcia-Herrero, A.,Vogel, H.J. (登録日: 2005-09-01, 公開日: 2005-12-27, 最終更新日: 2024-05-01)

主引用文献

Garcia-Herrero, A.,Vogel, H.J.
Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli
Mol.Microbiol., 58:1226-1237, 2005

PubMed Abstract: Gram-negative bacteria possess outer membrane receptors that utilize energy provided by the TonB system to take up iron. Several of these receptors participate in extracytoplasmic factor (ECF) signalling through an N-terminal signalling domain that interacts with a periplasmic transmembrane anti-sigma factor protein and a cytoplasmic sigma factor protein. The structures of the intact TonB-dependent outer membrane receptor FecA from Escherichia coli and FpvA from Pseudomonas aeruginosa have recently been solved by protein crystallography; however, no electron density was detected for their periplasmic signalling domains, suggesting that it was either unfolded or flexible with respect to the remainder of the protein. Here we describe the well-defined solution structure of this domain solved by multidimensional nuclear magnetic resonance (NMR) spectroscopy. The monomeric protein construct contains the 79-residue N-terminal domain as well as the next 17 residues that are part of the receptor's plug domain. These form two clearly distinct regions: a highly structured domain at the N-terminal end followed by an extended flexible tail at the C-terminal end, which includes the 'TonB-box' region, and connects it to the plug domain of the receptor. The structured region consists of two alpha-helices that are positioned side by side and are sandwiched in between two small beta-sheets. This is a novel protein fold which appears to be preserved in all the periplasmic signalling domains of bacterial TonB-dependent outer membrane receptors that are involved in ECF signalling, because the hydrophobic residues that make up the core of the protein domain are highly conserved.

PubMed: 16313612
DOI: 10.1111/j.1365-2958.2005.04889.x

実験手法

SOLUTION NMR