5mx4 | pdb_00005mx4

Crystal structure of H. pylori purine nucleoside phosphorylase from clinical isolate HpPNP-1

spinqualitylabelsall models 5mx4, resolution 2.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mx4 is a 6 chain structure with sequence from Helicobacter pylori R018c. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.31Å Ligands: HPA, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function K2JXG0_HELPX Publication Abstract from PubMed 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. Structural characterization of purine nucleoside phosphorylase from human pathogen Helicobacter pylori.,Stefanic Z, Mikleusevic G, Luic M, Bzowska A, Lescic Asler I Int J Biol Macromol. 2017 Mar 20;101:518-526. doi:, 10.1016/j.ijbiomac.2017.03.101. PMID:28336275 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Purine nucleoside phosphorylase 3D structures

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