Sugar-mediated lattice contacts in crystals of a plant glycoprotein

Tanis Hogg, Ivana Kuta Smatanova, Karel Bezouska, Norbert Ulbrich, Rolf Hilgenfeld*

*Corresponding author for this work
9 Citations (Scopus)


Pokeweed antiviral protein, PAP-Saci, isolated from seeds of the Chinese pokeweed plant, Phytolacca acinosa, belongs to the family of type-1 ribosome-inactivating proteins (RIPs). Type-1 RIPs are ∼30-kDa N-glycosidases that inactivate eukaryotic and prokaryotic ribosomes via a site-specific depurination of ribosomal RNA (rRNA). Here we describe the preliminary X-ray structure determination at 1.7 Å resolution of one PAP isoenzyme from seeds, PAP-S1aci, after crystallisation from a heterogeneous mixture of two isoenzymes. PAP-S1aci possesses a rare type of glycosylation, specifically, N-linked N-acetyl-D-glucosamine monosaccharide (GlcNAc) substitutions at canonical Asn-Xaa-Ser/Thr sequons. One GlcNAc residue was found to play a critical role in crystal lattice formation, forming a packing interface across a crystallographic two-fold with the identical sequon of an adjacent monomer. This observation suggests that deglycosylation protocols for the crystallisation of glycoproteins should be designed to allow for exploitation of the crystal packing potential of the innermost core sugar residue (N-linked GlcNAc or O-linked GalNAc).

Original languageEnglish
JournalActa Crystallographica Section D: Biological Crystallography
Issue number10 II
Pages (from-to)1734-1739
Number of pages6
Publication statusPublished - 01.10.2002

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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