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. 1999 May 14;284(5417):1171-4.
doi: 10.1126/science.284.5417.1171.

Crystal structure of a conserved ribosomal protein-RNA complex

G L Conn  1 , D E Draper, E E Lattman, A G Gittis
Affiliations

Crystal structure of a conserved ribosomal protein-RNA complex

G L Conn et al. Science. .

Abstract

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.

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