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Crystal structures of a new class of pyrimidine/purine nucleoside phosphorylase (ppnP) revealed a Cupin fold
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  • Yan Wen,
  • Xiaojia Li,
  • Wenting Guo,
  • Baixing Wu
Yan Wen
Sun Yat-Sen Memorial Hospital

Corresponding Author:[email protected]

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Xiaojia Li
Sun Yat-Sen Memorial Hospital
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Wenting Guo
Sun Yat-Sen Memorial Hospital
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Baixing Wu
Sun Yat-Sen Memorial Hospital
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Nucleotides metabolism is a fundamental process in all organisms. Two families of nucleoside phosphorylases (NP) that catalyze the phosphorolytic cleavage of the glycosidic bond in nucleosides have been found, including the trimeric or hexameric NP-I and dimeric NP-II family enzymes. Recently studies revealed another class of NP protein in E. coli named Pyrimidine/purine nucleoside phosphorylase (ppnP), which can catalyze the phosphorolysis of diverse nucleosides and yield D-ribose 1-phosphate and the respective free bases. Here, we solve the crystal structures of ppnP from E. coli and the other three species. Our studies revealed that the structure of ppnP belongs to the Rlmc-like cupin fold and showed as a rigid dimeric conformation. Detail analysis revealed a potential nucleoside binding pocket full of hydrophobic residues. And the residues involved in the dimer and pocket formation are all well conserved in bacteria. Since the cupin fold is a large superfamily in the biosynthesis of natural products, our studies provide the structural basis for understanding and the directed evolution of NP proteins.
14 Nov 2021Submitted to PROTEINS: Structure, Function, and Bioinformatics
16 Nov 2021Submission Checks Completed
16 Nov 2021Assigned to Editor
23 Nov 2021Reviewer(s) Assigned
29 Dec 2021Review(s) Completed, Editorial Evaluation Pending
31 Dec 2021Editorial Decision: Revise Minor
12 Jan 20221st Revision Received
12 Jan 2022Submission Checks Completed
12 Jan 2022Assigned to Editor
13 Jan 2022Reviewer(s) Assigned
21 Jan 2022Review(s) Completed, Editorial Evaluation Pending
24 Jan 2022Editorial Decision: Accept
Jun 2022Published in Proteins: Structure, Function, and Bioinformatics volume 90 issue 6 on pages 1233-1241. 10.1002/prot.26309