1jbr
Crystal Structure of the Ribotoxin Restrictocin and a 31-mer SRD RNA Inhibitor
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OverviewOverview
The cytotoxin sarcin disrupts elongation factor binding and protein, synthesis by specifically cleaving one phosphodiester bond in ribosomes., To elucidate the molecular basis of toxin action, we determined three, cocrystal structures of the sarcin homolog restrictocin bound to different, analogs that mimic the target sarcin/ricin loop (SRL) structure of the rat, 28S rRNA. In these structures, restrictocin contacts the bulged-G motif, and an unfolded form of the tetraloop of the SRL RNA. In one structure, toxin loops guide selection of the target site by contacting the base, critical for recognition (G4319) and the surrounding S-shaped backbone. In, another structure, base flipping of the tetraloop enables cleavage by, placing the target nucleotide in the active site with the nucleophile, nearly inline for attack on the scissile bond. These structures provide, the first views of how a site-specific protein endonuclease recognizes and, cleaves a folded RNA substrate.
About this StructureAbout this Structure
1JBR is a Single protein structure of sequence from Aspergillus restrictus with K as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of restrictocin-inhibitor complexes with implications for RNA recognition and base flipping., Yang X, Gerczei T, Glover LT, Correll CC, Nat Struct Biol. 2001 Nov;8(11):968-73. PMID:11685244
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