5WYO

Solution structure of E.coli HdeA

5WYO の概要

• エントリーDOI: 10.2210/pdb5wyo/pdb
• NMR情報: BMRB: 36045
• 分子名称: Acid stress chaperone HdeA (1 entity in total)
• 機能のキーワード: periplasmic protein, chaperone
• 由来する生物種: Escherichia coli O157:H7
• 細胞内の位置: Periplasm : P0AET0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19505.76

構造登録者

Yang, C.,Hu, Y.,Jin, C. (登録日: 2017-01-14, 公開日: 2017-11-22, 最終更新日: 2024-10-09)

主引用文献

Yu, X.C.,Yang, C.,Ding, J.,Niu, X.,Hu, Y.,Jin, C.
Characterizations of the Interactions between Escherichia coli Periplasmic Chaperone HdeA and Its Native Substrates during Acid Stress
Biochemistry, 56:5748-5757, 2017

PubMed Abstract: The bacterial acid-resistant chaperone HdeA is a "conditionally disordered" protein that functions at low pH when it undergoes a transition from a well-folded dimer to an unfolded monomer. The dimer dissociation and unfolding processes result in exposure of hydrophobic surfaces that allows binding to a broad range of client proteins. To fully elucidate the chaperone mechanism of HdeA, it is crucial to understand how the activated HdeA interacts with its native substrates during acid stress. Herein, we present a nuclear magnetic resonance study of the pH-dependent HdeA-substrate interactions. Our results show that the activation of HdeA is not only induced by acidification but also regulated by the presence of unfolded substrates. The variable extent of unfolding of substrates differentially regulates the HdeA-substrate interaction, and the binding further affects the HdeA conformation. Finally, we show that HdeA binds its substrates heterogeneously, and the "amphiphilic" model for HdeA-substrate interaction is discussed.

PubMed: 29016106
DOI: 10.1021/acs.biochem.7b00724

実験手法

SOLUTION NMR