5I3C

Crystal structure of E.coli purine nucleoside phosphorylase with acycloguanosine

Summary for 5I3C

• Entry DOI: 10.2210/pdb5i3c/pdb
• Descriptor: Purine nucleoside phosphorylase DeoD-type, 9-HYROXYETHOXYMETHYLGUANINE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: complex, transferase
• Biological source: Escherichia coli O139:H28 (strain E24377A / ETEC)
• Total number of polymer chains: 3
• Total formula weight: 78320.83

Authors

Timofeev, V.I.,Abramchik, Y.A.,Esipov, R.S.,Kuranova, I.P. (deposition date: 2016-02-10, release date: 2017-02-22, Last modification date: 2024-01-10)

Primary citation

Timofeev, V.I.,Zhukhlistova, N.E.,Abramchik, Y.A.,Muravieva, T.I.,Esipov, R.S.,Kuranova, I.P.
Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir.
Acta Crystallogr F Struct Biol Commun, 74:402-409, 2018

PubMed Abstract: Escherichia coli purine nucleoside phosphorylase (PNP), which catalyzes the reversible phosphorolysis of purine ribonucleosides, belongs to the family I hexameric PNPs. Owing to their key role in the purine salvage pathway, PNPs are attractive targets for drug design against some pathogens. Acyclovir (ACV) is an acyclic derivative of the PNP substrate guanosine and is used as an antiviral drug for the treatment of some human viral infections. The crystalline complex of E. coli PNP with acyclovir was prepared by co-crystallization in microgravity using counter-diffusion through a gel layer in a capillary. The structure of the E. coli PNP-ACV complex was solved at 2.32 Å resolution using the molecular-replacement method. The ACV molecule is observed in two conformations and sulfate ions were located in both the nucleoside-binding and phosphate-binding pockets of the enzyme. A comparison with the complexes of other hexameric and trimeric PNPs with ACV shows the similarity in acyclovir binding by these enzymes.

PubMed: 29969103
DOI: 10.1107/S2053230X18008087

Experimental method

X-RAY DIFFRACTION (2.32 Å)