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Crystal Structure of a Conserved Ribosomal Protein-RNA Complex

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Science  14 May 1999:
Vol. 284, Issue 5417, pp. 1171-1174
DOI: 10.1126/science.284.5417.1171

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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.

  • * To whom correspondence should be addressed. E-mail: draper{at}jhunix.hcf.jhu.edu and lattman{at}jhu.edu

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