Claim · model-written summary
The bRIP structure supports an enzymatic mechanism and reveals a new activation mechanism for cereal type I RIPs.
Not reportedTaxonMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Verbatim
e0“bRIP structure confirms the detailed enzymatic mechanism of this N-glycosidase and reveals a novel activation mechanism for type I RIPs from cereal crops”
Title
Byung-Gil Lee; Min Kyung Kim; Byeong-Won Kim; et al. Acta Crystallographica Section D Biological Crystallography 2012. doi:10.1107/s0907444912037110
Other claims from this paper (4)
- Observation Barley RIP has sequence features divergent from other plant RIP types.
- Observation The barley RIP structure has a fold similar to other RIPs but differs in specific regions.
- Mechanism A bRIP switch region shifts between a 3(10)-helix and loop according to liganded state.
- Observation The barley RIP switch region occupies the position of a putative ribosome-binding site in type III RIPs.