Structures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanism

Byung Gil Lee, Min Kyung Kim, Byeong Won Kim, Se Won Suh, Hyun Kyu Song

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


Ribosome-inactivating protein (RIP), a defence protein found in various plants, possesses different chain architectures and activation mechanisms. The RIP from barley (bRIP) is a type I RIP and has sequence features that are divergent from those of type I and type II RIPs from dicotyledonous plants and even the type III RIP from maize. This study presents the first crystal structure of an RIP from a cereal crop, barley, in free, AMP-bound and adenine-bound states. For phasing, a codon-optimized synthetic brip1 gene was used and a vector was constructed to overexpress soluble bRIP fusion proteins; such expression has been verified in a number of cases. The overall structure of bRIP shows folding similar to that observed in other RIPs but also shows significant differences in specific regions, particularly in a switch region that undergoes a structural transition between a 310-helix and a loop depending on the liganded state. The switch region is in a position equivalent to that of a proteolytically susceptible and putative ribosome-binding site in type III RIPs. Thus, the bRIP structure confirms the detailed enzymatic mechanism of this N-glycosidase and reveals a novel activation mechanism for type I RIPs from cereal crops.

Original languageEnglish
Pages (from-to)1488-1500
Number of pages13
JournalActa Crystallographica Section D: Biological Crystallography
Issue number11
Publication statusPublished - 2012 Nov


  • RIP
  • barley
  • cereal crops
  • monocots
  • surface-entropy reduction

ASJC Scopus subject areas

  • Structural Biology


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