Crystal structure of pokeweed antiviral protein with well-defined sugars from seeds at 1.8 Å resolution

Zong Hao Zeng, Xiao Lin He, Hong Min Li, Zhong Hu, Da Cheng Wang*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


The crystal structure of pokeweed antiviral protein from seeds of Phytolacca americana (PAP-S) was solved at 1.8Å. PAP-S is a one-chain ribosome-inactivating protein (RIP) and distinctively contains three well-defined N-acetylglucosamines, each covalently linked to an asparagine residue at positions, 10, 44, and 255, respectively. The high-resolution structure clearly shows the three mono-sugars to have either an α- or a β-conformation. Two of sugars are located on the same side of the molecule with the active pocket. Except one hydrogen bond, there are no intermolecular interactions between the polypeptide chain and the sugars. Instead the sugar conformations appear to be stabilized by intermolecular interactions. The sugar structure defined at high resolution provides a structural basis for understanding their possible biological activity. The structural comparisons of PAP-S with other PAPs reveal that the major disparity of these homologous molecules is the different charge distribution on the upper right side of the front side near the active pocket. Based on the available structure of the 50S ribosomal subunit, the possible interactions between PAPs and the ribosome are discussed.

Original languageEnglish (US)
Pages (from-to)171-178
Number of pages8
JournalJournal of Structural Biology
Issue number2
StatePublished - Feb 1 2003


  • Crystal structure
  • N-Acetylglucosamine
  • Pokeweed antiviral protein
  • Ribosome-inactivating protein

ASJC Scopus subject areas

  • Structural Biology


Dive into the research topics of 'Crystal structure of pokeweed antiviral protein with well-defined sugars from seeds at 1.8 Å resolution'. Together they form a unique fingerprint.

Cite this