2D2R

Crystal structure of Helicobacter pylori Undecaprenyl Pyrophosphate Synthase

2D2R の概要

• エントリーDOI: 10.2210/pdb2d2r/pdb
• 分子名称: Undecaprenyl Pyrophosphate Synthase (2 entities in total)
• 機能のキーワード: prenyl, prenyltransferase, undecaprenyl, transferase
• 由来する生物種: Helicobacter pylori
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57151.85

構造登録者

Kuo, C.J.,Guo, R.T.,Chen, C.L.,Ko, T.P.,Cheng, Y.S.,Cheng, Y.L.,Liang, P.H.,Wang, A.H.-J. (登録日: 2005-09-16, 公開日: 2006-09-26, 最終更新日: 2023-10-25)

主引用文献

Kuo, C.J.,Guo, R.T.,Lu, I.L.,Liu, H.G.,Wu, S.Y.,Ko, T.P.,Wang, A.H.,Liang, P.H.
Structure-based inhibitors exhibit differential activities against Helicobacter pylori and Escherichia coli undecaprenyl pyrophosphate synthases.
J.Biomed.Biotechnol., 2008:841312-841312, 2008

PubMed Abstract: Helicobacter pylori colonizes the human gastric epithelium and causes diseases such as gastritis, peptic ulcers, and stomach cancer. Undecaprenyl pyrophosphate synthase (UPPS), which catalyzes consecutive condensation reactions of farnesyl pyrophosphate with eight isopentenyl pyrophosphate to form lipid carrier for bacterial peptidoglycan biosynthesis, represents a potential target for developing new antibiotics. In this study, we solved the crystal structure of H. pylori UPPS and performed virtual screening of inhibitors from a library of 58,635 compounds. Two hits were found to exhibit differential activities against Helicobacter pylori and Escherichia coli UPPS, giving the possibility of developing antibiotics specially targeting pathogenic H. pylori without killing the intestinal E. coli.

PubMed: 18382620
DOI: 10.1155/2008/841312

実験手法

X-RAY DIFFRACTION (1.88 Å)