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Publication Abstract from PubMed

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 3(10)-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.

Structures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanism.,Lee BG, Kim MK, Kim BW, Suh SW, Song HK Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1488-500. doi:, 10.1107/S0907444912037110. Epub 2012 Oct 13. PMID:23090398^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.