Crystal Structure of a Conserved Ribosomal Protein-RNA Complex
- 14 May 1999
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 284 (5417) , 1171-1174
- https://doi.org/10.1126/science.284.5417.1171
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.Keywords
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