6E55

1.57 Angstroem Crystal Structure of FeoA from Klebsiella pneumoniae

6E55 の概要

• エントリーDOI: 10.2210/pdb6e55/pdb
• 分子名称: FeoA protein (2 entities in total)
• 機能のキーワード: iron transport, protein-protein interactions, protein regulation, transport protein
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 61943.24

構造登録者

Linkous, R.O.,Sestok, A.E.,Smith, A.T. (登録日: 2018-07-19, 公開日: 2019-06-12, 最終更新日: 2024-03-13)

主引用文献

Linkous, R.O.,Sestok, A.E.,Smith, A.T.
The crystal structure of Klebsiella pneumoniae FeoA reveals a site for protein-protein interactions.
Proteins, 87:897-903, 2019

PubMed Abstract: In order to establish infection, pathogenic bacteria must obtain essential nutrients such as iron. Under acidic and/or anaerobic conditions, most bacteria utilize the Feo system in order to acquire ferrous iron (Fe ) from their host environment. The mechanism of this process, including its regulation, remains poorly understood. In this work, we have determined the crystal structure of FeoA from the nosocomial agent Klebsiella pneumoniae (KpFeoA). Our structure reveals an SH3-like domain that mediates interactions between neighboring polypeptides via hydrophobic intercalations into a Leu-rich surface ridge. Using docking of a small peptide corresponding to a postulated FeoB partner binding site, we demonstrate that KpFeoA can assume both "open" and "closed" conformations, controlled by binding at this Leu-rich ridge. We propose a model in which a "C-shaped" clamp along the FeoA surface mediates interactions with its partner protein, FeoB. These findings are the first to demonstrate atomic-level details of FeoA-based protein-protein interactions and provide a framework for testing FeoA-FeoB interactions, which could be exploited for future antibiotic developments.

PubMed: 31162843
DOI: 10.1002/prot.25755

実験手法

X-RAY DIFFRACTION (1.57 Å)