5I3C

Crystal structure of E.coli purine nucleoside phosphorylase with acycloguanosine

5I3C の概要

• エントリーDOI: 10.2210/pdb5i3c/pdb
• 分子名称: Purine nucleoside phosphorylase DeoD-type, 9-HYROXYETHOXYMETHYLGUANINE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: complex, transferase
• 由来する生物種: Escherichia coli O139:H28 (strain E24377A / ETEC)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 78320.83

構造登録者

Timofeev, V.I.,Abramchik, Y.A.,Esipov, R.S.,Kuranova, I.P. (登録日: 2016-02-10, 公開日: 2017-02-22, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.32 Å)