2D2R

Crystal structure of Helicobacter pylori Undecaprenyl Pyrophosphate Synthase

Summary for 2D2R

• Entry DOI: 10.2210/pdb2d2r/pdb
• Descriptor: Undecaprenyl Pyrophosphate Synthase (2 entities in total)
• Functional Keywords: prenyl, prenyltransferase, undecaprenyl, transferase
• Biological source: Helicobacter pylori
• Total number of polymer chains: 2
• Total formula weight: 57151.85

Authors

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. (deposition date: 2005-09-16, release date: 2006-09-26, Last modification date: 2023-10-25)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.88 Å)