5MX8

Crystal structure of H. pylori purine nucleoside phosphorylase from clinical isolate HpPNP-3

Summary for 5MX8

• Entry DOI: 10.2210/pdb5mx8/pdb
• Related: 5MX4 5MX6
• Descriptor: Purine nucleoside phosphorylase DeoD-type, HYPOXANTHINE, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: purine nucleoside phosphorylase, clinical isolate, helicobacter pylori, dead-end-complex, transferase
• Biological source: Helicobacter pylori
• Total number of polymer chains: 1
• Total formula weight: 27601.99

Authors

Stefanic, Z. (deposition date: 2017-01-21, release date: 2017-04-05, Last modification date: 2024-01-17)

Primary citation

Stefanic, Z.,Mikleusevic, G.,Luic, M.,Bzowska, A.,Lescic Asler, I.
Structural characterization of purine nucleoside phosphorylase from human pathogen Helicobacter pylori.
Int. J. Biol. Macromol., 101:518-526, 2017

PubMed Abstract: Microaerophilic bacterium Helicobacer pylori is a well known human pathogen involved in the development of many diseases. Due to the evergrowing infection rate and increase of H. pylori antibiotic resistence, it is of utmost importance to find a new way to attack and eradicate H. pylori. The purine metabolism in H. pylori is solely dependant on the salvage pathway and one of the key enzymes in this pathway is purine nucleoside phosphorylase (PNP). In this timely context, we report here the basic biochemical and structural characterization of recombinant PNP from the H. pylori clinical isolate expressed in Escherichia coli. Structure of H. pylori PNP is typical for high molecular mass PNPs. However, its activity towards adenosine is very low, thus resembling more that of low molecular mass PNPs. Understanding the molecular mechanism of this key enzyme may lead to the development of new drug strategies and help in the eradication of H. pylori.

PubMed: 28336275
DOI: 10.1016/j.ijbiomac.2017.03.101

Experimental method

X-RAY DIFFRACTION (2.4 Å)