8HC1

CryoEM structure of Helicobacter pylori UreFD/urease complex

これはPDB形式変換不可エントリーです。

8HC1 の概要

• エントリーDOI: 10.2210/pdb8hc1/pdb
• EMDBエントリー: 34648 34659
• 分子名称: Urease subunit alpha, Urease subunit beta, Urease accessory protein UreH, ... (4 entities in total)
• 機能のキーワード: urease, activation complex, urea, ureb, urec, uref, ured, ureh, helicobacter pylori, hydrolase
• 由来する生物種: Helicobacter pylori 26695; 詳細
• タンパク質・核酸の鎖数: 48
• 化学式量合計: 1771272.59

構造登録者

Nim, Y.S.,Fong, I.Y.H.,Deme, J.,Tsang, K.L.,Caesar, J.,Johnson, S.,Wong, K.B.,Lea, S.M. (登録日: 2022-11-01, 公開日: 2023-05-03, 最終更新日: 2024-06-19)

主引用文献

Nim, Y.S.,Fong, I.Y.H.,Deme, J.,Tsang, K.L.,Caesar, J.,Johnson, S.,Pang, L.T.H.,Yuen, N.M.H.,Ng, T.L.C.,Choi, T.,Wong, Y.Y.H.,Lea, S.M.,Wong, K.B.
Delivering a toxic metal to the active site of urease.
Sci Adv, 9:eadf7790-eadf7790, 2023

PubMed Abstract: Urease is a nickel (Ni) enzyme that is essential for the colonization of in the human stomach. To solve the problem of delivering the toxic Ni ion to the active site without diffusing into the cytoplasm, cells have evolved metal carrier proteins, or metallochaperones, to deliver the toxic ions to specific protein complexes. Ni delivery requires urease to form an activation complex with the urease accessory proteins UreFD and UreG. Here, we determined the cryo-electron microscopy structures of UreFD/urease and UreD/urease complexes at 2.3- and 2.7-angstrom resolutions, respectively. Combining structural, mutagenesis, and biochemical studies, we show that the formation of the activation complex opens a 100-angstrom-long tunnel, where the Ni ion is delivered through UreFD to the active site of urease.

PubMed: 37083535
DOI: 10.1126/sciadv.adf7790

実験手法

ELECTRON MICROSCOPY (2.3 Å)