1sds
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Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA
OverviewOverview
The archaeal RNA binding protein L7Ae and its eukaryotic homolog 15.5, kDa/Snu13 recognize K-turns. This structural motif is canonically, comprised of two stems (one with tandem A.G base pairs, the other with, Watson-Crick pairs) linked by an asymmetric internal loop. L7Ae recognizes, conventional K-turns in ribosomal and box C/D RNAs but also binds, specifically to some box H/ACA RNAs at terminal stem loops. These have the, A.G paired stem, but lack the Watson-Crick stem. The structure of, Methanococcus jannaschii L7Ae bound to a symmetric duplex RNA without, Watson-Crick stems demonstrates how a binding site for this component of, diverse ribonucleoprotein complexes can be constructed with only the A.G, stem and the loop. The RNA adopts a functional conformation with the aid, of a base triple and tight binding of divalent cations. Comparison with, the 15.5 kDa/Snu13-RNA complex structure suggests why the eukaryotic, homolog does not recognize terminal stem loop L7Ae binding sites.
About this StructureAbout this Structure
1SDS is a Single protein structure of sequence from Methanocaldococcus jannaschii with CA and K as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 A resolution., Hamma T, Ferre-D'Amare AR, Structure. 2004 May;12(5):893-903. PMID:15130481
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