2XUV

The structure of HdeB

2XUV の概要

• エントリーDOI: 10.2210/pdb2xuv/pdb
• 分子名称: HDEB, SULFATE ION (3 entities in total)
• 機能のキーワード: unknown function
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 37354.47

構造登録者

Naismith, J.H.,Wang, W. (登録日: 2010-10-21, 公開日: 2011-08-24, 最終更新日: 2025-04-09)

主引用文献

Wang, W.,Rasmussen, T.,Harding, A.J.,Booth, N.A.,Booth, I.R.,Naismith, J.H.
Salt Bridges Regulate Both Dimer Formation and Monomeric Flexibility in Hdeb and May Have a Role in Periplasmic Chaperone Function.
J.Mol.Biol., 415:538-, 2012

PubMed Abstract: Escherichia coli and Gram-negative bacteria that live in the human gut must be able to tolerate rapid and large changes in environmental pH. Low pH irreversibly denatures and precipitates many bacterial proteins. While cytoplasmic proteins are well buffered against such swings, periplasmic proteins are not. Instead, it appears that some bacteria utilize chaperone proteins that stabilize periplasmic proteins, preventing their precipitation. Two highly expressed and related proteins, HdeA and HdeB, have been identified as acid-activated chaperones. The structure of HdeA is known and a mechanism for activation has been proposed. In this model, dimeric HdeA dissociates at low pH, and the exposed dimeric interface binds exposed hydrophobic surfaces of acid-denatured proteins, preventing their irreversible aggregation. We now report the structure and biophysical characterization of the HdeB protein. The monomer of HdeB shares a similar structure with HdeA, but its dimeric interface is different in composition and spatial location. We have used fluorescence to study the behavior of HdeB as pH is lowered, and like HdeA, it dissociates to monomers. We have identified one of the key intersubunit interactions that controls pH-induced monomerization. Our analysis identifies a structural interaction within the HdeB monomer that is disrupted as pH is lowered, leading to enhanced structural flexibility.

PubMed: 22138344
DOI: 10.1016/J.JMB.2011.11.026

実験手法

X-RAY DIFFRACTION (1.5 Å)