4FBB
Structure of mutant RIP from barley seeds in complex with adenine (AMP-incubated)
Summary for 4FBB
| Entry DOI | 10.2210/pdb4fbb/pdb |
| Related | 4FB9 4FBA 4FBC 4FBH |
| Descriptor | Protein synthesis inhibitor I, ADENINE (3 entities in total) |
| Functional Keywords | hydrolase, ribosome inactivating protein, rrna n-glycosylase activity, ribosome |
| Biological source | Hordeum vulgare (barley) |
| Cellular location | Cytoplasm: P22244 |
| Total number of polymer chains | 4 |
| Total formula weight | 119806.34 |
| Authors | Lee, B.-G.,Kim, M.K.,Suh, S.W.,Song, H.K. (deposition date: 2012-05-22, release date: 2012-10-31, Last modification date: 2024-02-28) |
| Primary citation | Lee, B.G.,Kim, M.K.,Kim, B.W.,Suh, S.W.,Song, H.K. Structures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanism. Acta Crystallogr.,Sect.D, 68:1488-1500, 2012 Cited by PubMed 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. PubMed: 23090398DOI: 10.1107/S0907444912037110 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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