4fbh: Difference between revisions
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==Structure of RIP from barley seeds== | ==Structure of RIP from barley seeds== | ||
<StructureSection load='4fbh' size='340' side='right' caption='[[4fbh]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4fbh' size='340' side='right'caption='[[4fbh]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FBH FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fbh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FBH FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Hordeum vulgare]] | [[Category: Hordeum vulgare]] | ||
[[Category: Large Structures]] | |||
[[Category: RRNA N-glycosylase]] | [[Category: RRNA N-glycosylase]] | ||
[[Category: Kim, M K]] | [[Category: Kim, M K]] | ||
Revision as of 13:02, 5 February 2020
Structure of RIP from barley seedsStructure of RIP from barley seeds
Structural highlights
Function[RIP1_HORVU] Inhibits the elongation phase of protein synthesis. It inactivates fungal ribosomes even more effectively than mammalian ribosomes and is thought to function as a constitutive antifungal agent in plants. Publication Abstract from PubMedRibosome-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. References
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