2MYJ

Solution structure of a bacterial chaperone

2MYJ の概要

• エントリーDOI: 10.2210/pdb2myj/pdb
• NMR情報: BMRB: 25454
• 分子名称: Acid stress chaperone HdeB (1 entity in total)
• 機能のキーワード: chaperone
• 由来する生物種: Escherichia coli K-12
• 細胞内の位置: Periplasm : P0AET2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18148.43

構造登録者

Jin, C.,Hu, Y.,Ding, J. (登録日: 2015-01-27, 公開日: 2016-01-06, 最終更新日: 2024-11-27)

主引用文献

Ding, J.,Yang, C.,Niu, X.,Hu, Y.,Jin, C.
HdeB chaperone activity is coupled to its intrinsic dynamic properties.
Sci Rep, 5:16856-16856, 2015

PubMed Abstract: Enteric bacteria encounter extreme acidity when passing through hosts' stomach. Since the bacterial periplasmic space quickly equilibrates with outer environment, an efficient acid resistance mechanism is essential in preventing irreversible protein denaturation/aggregation and maintaining bacteria viability. HdeB, along with its homolog HdeA, was identified as a periplasmic acid-resistant chaperone. Both proteins exist as homodimers and share similar monomeric structures under neutral pH, while showing different dimeric packing interfaces. Previous investigations show that HdeA functions through an acid-induced dimer-to-monomer transition and partial unfolding at low pH (pH 2-3), resulting in exposure of hydrophobic surfaces that bind substrate proteins. In contrast, HdeB appears to have a much higher optimal activation pH (pH 4-5), under which condition the protein maintains a well-folded dimer and the mechanism for its chaperone activity remains elusive. Herein, we present an NMR study of HdeB to investigate its dynamic properties. Our results reveal that HdeB undergoes significant micro- to milli-second timescale conformational exchanges at neutral to near-neutral pH, under the later condition it exhibits optimal activity. The current study indicates that HdeB activation is coupled to its intrinsic dynamics instead of structural changes, and therefore its functional mechanism is apparently different from HdeA.

PubMed: 26593705
DOI: 10.1038/srep16856

実験手法

SOLUTION NMR