4HI0

Crystal Structure of Helicobacter pylori Urease Accessory Protein UreF/H/G complex

4HI0 の概要

• エントリーDOI: 10.2210/pdb4hi0/pdb
• 関連するPDBエントリー: 2WGL 3O1Q 3SF5
• 分子名称: Urease accessory protein UreF, Urease accessory protein UreH, Urease accessory protein UreG, ... (5 entities in total)
• 機能のキーワード: metallochaperone, metal binding protein, urease, cytosol
• 由来する生物種: Helicobacter pylori; 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q09065 Q09067 Q09066
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 161671.01

構造登録者

Fong, Y.H.,Chen, Y.W.,Wong, K.B. (登録日: 2012-10-11, 公開日: 2013-10-16, 最終更新日: 2024-02-28)

主引用文献

Fong, Y.H.,Wong, H.C.,Yuen, M.H.,Lau, P.H.,Chen, Y.W.,Wong, K.B.
Structure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori urease.
Plos Biol., 11:e1001678-e1001678, 2013

PubMed Abstract: Urease is a metalloenzyme essential for the survival of Helicobacter pylori in acidic gastric environment. Maturation of urease involves carbamylation of Lys219 and insertion of two nickel ions at its active site. This process requires GTP hydrolysis and the formation of a preactivation complex consisting of apo-urease and urease accessory proteins UreF, UreH, and UreG. UreF and UreH form a complex to recruit UreG, which is a SIMIBI class GTPase, to the preactivation complex. We report here the crystal structure of the UreG/UreF/UreH complex, which illustrates how UreF and UreH facilitate dimerization of UreG, and assembles its metal binding site by juxtaposing two invariant Cys66-Pro67-His68 metal binding motif at the interface to form the (UreG/UreF/UreH)2 complex. Interaction studies revealed that addition of nickel and GTP to the UreG/UreF/UreH complex releases a UreG dimer that binds a nickel ion at the dimeric interface. Substitution of Cys66 and His68 with alanine abolishes the formation of the nickel-charged UreG dimer. This nickel-charged UreG dimer can activate urease in vitro in the presence of the UreF/UreH complex. Static light scattering and atomic absorption spectroscopy measurements demonstrated that the nickel-charged UreG dimer, upon GTP hydrolysis, reverts to its monomeric form and releases nickel to urease. Based on our results, we propose a mechanism on how urease accessory proteins facilitate maturation of urease.

PubMed: 24115911
DOI: 10.1371/journal.pbio.1001678

実験手法

X-RAY DIFFRACTION (2.35 Å)