6X84

Sn-glycerol-3-phosphate binding periplasmic protein UgpB from Escherichia coli - W169S, W172S

6X84 の概要

• エントリーDOI: 10.2210/pdb6x84/pdb
• 分子名称: sn-glycerol-3-phosphate-binding periplasmic protein UgpB, GLYCEROL (3 entities in total)
• 機能のキーワード: chaperone
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92219.27

構造登録者

Wu, K.,Zyla, D.,Bardwell, J.C.A. (登録日: 2020-06-01, 公開日: 2020-08-19, 最終更新日: 2023-10-18)

主引用文献

Lee, C.,Betschinger, P.,Wu, K.,Zyla, D.S.,Glockshuber, R.,Bardwell, J.C.
A metabolite binding protein moonlights as a bile-responsive chaperone.
Embo J., 39:e104231-e104231, 2020

PubMed Abstract: Bile salts are secreted into the gastrointestinal tract to aid in the absorption of lipids. In addition, bile salts show potent antimicrobial activity in part by mediating bacterial protein unfolding and aggregation. Here, using a protein folding sensor, we made the surprising discovery that the Escherichia coli periplasmic glycerol-3-phosphate (G3P)-binding protein UgpB can serve, in the absence of its substrate, as a potent molecular chaperone that exhibits anti-aggregation activity against bile salt-induced protein aggregation. The substrate G3P, which is known to accumulate in the later compartments of the digestive system, triggers a functional switch between UgpB's activity as a molecular chaperone and its activity as a G3P transporter. A UgpB mutant unable to bind G3P is constitutively active as a chaperone, and its crystal structure shows that it contains a deep surface groove absent in the G3P-bound wild-type UgpB. Our work illustrates how evolution may be able to convert threats into signals that first activate and then inactivate a chaperone at the protein level in a manner that bypasses the need for ATP.

PubMed: 32882062
DOI: 10.15252/embj.2019104231

実験手法

X-RAY DIFFRACTION (1.25 Å)