6QSU

Helicobacter pylori urease with BME bound in the active site

6QSU の概要

• エントリーDOI: 10.2210/pdb6qsu/pdb
• 関連するPDBエントリー: 6QSU
• EMDBエントリー: 4629
• 分子名称: Urease subunit alpha, Urease subunit beta, NICKEL (II) ION, ... (5 entities in total)
• 機能のキーワード: dodecamer, bi nickel center, enzyme, cytoplasm, hydrolase
• 由来する生物種: Helicobacter pylori; 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 1064085.04

構造登録者

Luecke, H.,Cunha, E. (登録日: 2019-02-22, 公開日: 2021-01-20, 最終更新日: 2025-04-09)

主引用文献

Cunha, E.S.,Chen, X.,Sanz-Gaitero, M.,Mills, D.J.,Luecke, H.
Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 angstrom resolution.
Nat Commun, 12:230-230, 2021

PubMed Abstract: Infection of the human stomach by Helicobacter pylori remains a worldwide problem and greatly contributes to peptic ulcer disease and gastric cancer. Without active intervention approximately 50% of the world population will continue to be infected with this gastric pathogen. Current eradication, called triple therapy, entails a proton-pump inhibitor and two broadband antibiotics, however resistance to either clarithromycin or metronidazole is greater than 25% and rising. Therefore, there is an urgent need for a targeted, high-specificity eradication drug. Gastric infection by H. pylori depends on the expression of a nickel-dependent urease in the cytoplasm of the bacteria. Here, we report the 2.0 Å resolution structure of the 1.1 MDa urease in complex with an inhibitor by cryo-electron microscopy and compare it to a β-mercaptoethanol-inhibited structure at 2.5 Å resolution. The structural information is of sufficient detail to aid in the development of inhibitors with high specificity and affinity.

PubMed: 33431861
DOI: 10.1038/s41467-020-20485-6

実験手法

ELECTRON MICROSCOPY (2.4 Å)