CRYSTAL STRUCTURE OF A CONSERVED RIBOSOMAL PROTEIN-RNA COMPLEX

File:1qa6.gif


1qa6, resolution 2.800Å

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OverviewOverview

The structure of a highly conserved complex between a 58-nucleotide domain of large subunit ribosomal RNA and the RNA-binding domain of ribosomal protein L11 has been solved at 2.8 angstrom resolution. It reveals a precisely folded RNA structure that is stabilized by extensive tertiary contacts and contains an unusually large core of stacked bases. A bulge loop base from one hairpin of the RNA is intercalated into the distorted major groove of another helix; the protein locks this tertiary interaction into place by binding to the intercalated base from the minor groove side. This direct interaction with a key ribosomal RNA tertiary interaction suggests that part of the role of L11 is to stabilize an unusual RNA fold within the ribosome.

About this StructureAbout this Structure

1QA6 is a Single protein structure of sequence from Geobacillus stearothermophilus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a conserved ribosomal protein-RNA complex., Conn GL, Draper DE, Lattman EE, Gittis AG, Science. 1999 May 14;284(5417):1171-4. PMID:10325228

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