Structures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanism
- Authors
- Lee, Byung-Gil; Kim, Min Kyung; Kim, Byeong-Won; Suh, Se Won; Song, Hyun Kyu
- Issue Date
- 11월-2012
- Publisher
- INT UNION CRYSTALLOGRAPHY
- Keywords
- barley; cereal crops; monocots; RIP; surface-entropy reduction
- Citation
- ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, v.68, pp.1488 - 1500
- Indexed
- SCIE
SCOPUS
- Journal Title
- ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
- Volume
- 68
- Start Page
- 1488
- End Page
- 1500
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/107108
- DOI
- 10.1107/S0907444912037110
- ISSN
- 2059-7983
- Abstract
- 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.
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