Crystal Structure of a Conserved Ribosomal Protein-RNA Complex
Graeme L. Conn,
1
David E. Draper,
1*
Eaton E. Lattman,
2*
Apostolos G. Gittis
2
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.
1 Department of Chemistry and
2 Department of Biophysics, Johns Hopkins
University, Baltimore, MD 21218, USA.
*
To whom correspondence should be addressed. E-mail:
draper{at}jhunix.hcf.jhu.edu and lattman{at}jhu.edu
