5DH0

Structure of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca in P41

5DH0 の概要

• エントリーDOI: 10.2210/pdb5dh0/pdb
• 関連するPDBエントリー: 5DH1 5DH2
• 分子名称: siderophore periplasmic binding protein (2 entities in total)
• 機能のキーワード: siderophore, periplasmic binding protein, fuscachelin, protein binding
• 由来する生物種: Thermobifida fusca (strain YX)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67470.27

構造登録者

Li, K.,Bruner, S.D. (登録日: 2015-08-29, 公開日: 2015-11-18, 最終更新日: 2024-03-06)

主引用文献

Li, K.,Bruner, S.D.
Structure and functional analysis of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca.
Proteins, 84:118-128, 2016

PubMed Abstract: Iron acquisition is a complex, multicomponent process critical for most organisms' survival and virulence. Small iron chelating molecules, siderophores, mediate transport as key components of common pathways for iron assimilation in many microorganisms. The chemistry and biology of the extraordinary tight and specific metal binding siderophores is of general interest in terms of host/guest chemistry and is a potential target toward the development of therapeutic treatments for microbial virulence. The siderophore pathway of the moderate thermophile, Thermobifida fusca, is an excellent model system to study the process in Gram-positive bacteria. Here we describe the structure and characterization of the siderophore periplasmic binding protein, FscJ from the fuscachelin gene cluster of T. fusca. The structure shows a di-domain arrangement connected with a long α-helix hinge. Several X-ray structures detail ligand-free conformational changes at different pH values, illustrating complex interdomain flexibility of the siderophore receptors. We demonstrated that FscJ has a unique recognition mechanism and details the binding interaction with ferric-fuscachelin A through ITC and docking analysis. The presented work provides a structural basis for the complex molecular mechanisms of siderophore recognition and transportation.

PubMed: 26537767
DOI: 10.1002/prot.24959

実験手法

X-RAY DIFFRACTION (2.444 Å)