1sds

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File:1sds.gif


1sds, resolution 1.80Å

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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 and 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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