6YL3

High resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica

これはPDB形式変換不可エントリーです。

6YL3 の概要

• エントリーDOI: 10.2210/pdb6yl3/pdb
• EMDBエントリー: 10835
• 分子名称: Urease subunit gamma, Urease subunit beta, Urease subunit alpha, ... (5 entities in total)
• 機能のキーワード: urease, enzyme, nickel, metalloenzyme, pathogen, metal binding protein
• 由来する生物種: Yersinia enterocolitica W22703; 詳細
• タンパク質・核酸の鎖数: 36
• 化学式量合計: 1042168.79

構造登録者

Righetto, R.D.,Anton, L.,Adaixo, R.,Jakob, R.,Zivanov, J.,Mahi, M.A.,Ringler, P.,Schwede, T.,Maier, T.,Stahlberg, H. (登録日: 2020-04-06, 公開日: 2020-05-06, 最終更新日: 2025-04-09)

主引用文献

Righetto, R.D.,Anton, L.,Adaixo, R.,Jakob, R.P.,Zivanov, J.,Mahi, M.A.,Ringler, P.,Schwede, T.,Maier, T.,Stahlberg, H.
High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica.
Nat Commun, 11:5101-5101, 2020

PubMed Abstract: Urease converts urea into ammonia and carbon dioxide and makes urea available as a nitrogen source for all forms of life except animals. In human bacterial pathogens, ureases also aid in the invasion of acidic environments such as the stomach by raising the surrounding pH. Here, we report the structure of urease from the pathogen Yersinia enterocolitica at 2 Å resolution from cryo-electron microscopy. Y. enterocolitica urease is a dodecameric assembly of a trimer of three protein chains, ureA, ureB and ureC. The high data quality enables detailed visualization of the urease bimetal active site and of the impact of radiation damage. The obtained structure is of sufficient quality to support drug development efforts.

PubMed: 33037208
DOI: 10.1038/s41467-020-18870-2

実験手法

ELECTRON MICROSCOPY (1.98 Å)