3CXN

Structure of the Urease Accessory Protein UreF from Helicobacter pylori

3CXN の概要

• エントリーDOI: 10.2210/pdb3cxn/pdb
• 分子名称: Urease accessory protein ureF, GLYCEROL (3 entities in total)
• 機能のキーワード: helical, nickel, chaperone
• 由来する生物種: Helicobacter pylori (Campylobacter pylori)
• 細胞内の位置: Cytoplasm : Q09065
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 94109.19

構造登録者

Lam, R.,Johns, K.,Romanov, V.,Dong, A.,Wu-Brown, J.,Guthrie, J.,Dharamsi, A.,Thambipillai, D.,Mansoury, K.,Edwards, A.M.,Pai, E.F.,Chirgadze, N.Y. (登録日: 2008-04-24, 公開日: 2009-05-12, 最終更新日: 2024-10-09)

主引用文献

Lam, R.,Romanov, V.,Johns, K.,Battaile, K.P.,Wu-Brown, J.,Guthrie, J.L.,Hausinger, R.P.,Pai, E.F.,Chirgadze, N.Y.
Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori.
Proteins, 78:2839-2848, 2010

PubMed Abstract: Urease plays a central role in the pathogenesis of Helicobacter pylori in humans. Maturation of this nickel metalloenzyme in bacteria requires the participation of the accessory proteins UreD (termed UreH in H. pylori), UreF, and UreG, which form sequential complexes with the urease apoprotein as well as UreE, a metallochaperone. Here, we describe the crystal structure of C-terminal truncated UreF from H. pylori (residues 1-233), the first UreF structure to be determined, at 1.55 A resolution using SAD methods. UreF forms a dimer in vitro and adopts an all-helical fold congruent with secondary structure prediction. On the basis of evolutionary conservation analysis, the structure reveals a probable binding surface for interaction with other urease components as well as key conserved residues of potential functional relevance.

PubMed: 20635345
DOI: 10.1002/prot.22802

実験手法

X-RAY DIFFRACTION (1.55 Å)