7OOZ

Purine nucleoside phosphorylase(DeoD-type) from H. pylori with 6-benzyloxo-2-chloropurine

Summary for 7OOZ

• Entry DOI: 10.2210/pdb7ooz/pdb
• Descriptor: Purine nucleoside phosphorylase DeoD-type, GLYCEROL, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: inhibitor, complex, transferase
• Biological source: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
• Total number of polymer chains: 2
• Total formula weight: 53796.00

Authors

Narczyk, M.,Stefanic, Z. (deposition date: 2021-05-28, release date: 2022-05-04, Last modification date: 2024-11-20)

Primary citation

Narczyk, M.,Wojtys, M.I.,Lescic Asler, I.,Zinic, B.,Luic, M.,Jagusztyn-Krynicka, E.K.,Stefanic, Z.,Bzowska, A.
Interactions of 2,6-substituted purines with purine nucleoside phosphorylase from Helicobacter pylori in solution and in the crystal, and the effects of these compounds on cell cultures of this bacterium.
J Enzyme Inhib Med Chem, 37:1083-1097, 2022

PubMed Abstract: represents a global health threat with around 50% of the world population infected. Due to the increasing number of antibiotic-resistant strains, new strategies for eradication of are needed. In this study, we suggest purine nucleoside phosphorylase (PNP) as a possible new drug target, by characterising its interactions with 2- and/or 6-substituted purines as well as the effect of these compounds on bacterial growth. Inhibition constants are in the micromolar range, the lowest being that of 6-benzylthio-2-chloropurine. This compound also inhibits 26695 growth at the lowest concentration. X-ray structures of the complexes of PNP with the investigated compounds allowed the identification of interactions of inhibitors in the enzyme's base-binding site and the suggestion of structures that could bind to the enzyme more tightly. Our findings prove the potential of PNP inhibitors in the design of drugs against .

PubMed: 35437103
DOI: 10.1080/14756366.2022.2061965

Experimental method

X-RAY DIFFRACTION (1.7 Å)