Summary information and primary citation
- PDB-id
-
1mzp;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- ribosome
- Method
- X-ray (2.65 Å)
- Summary
- Structure of the l1 protuberance in the ribosome
- Reference
-
Nikulin A, Eliseikina I, Tishchenko S, Nevskaya N,
Davydova N, Platonova O, Piendl W, Selmer M, Liljas A,
Drygin D, Zimmermann R, Garber M, Nikonov S (2003):
"Structure
of the L1 protuberance in the ribosome."
Nat.Struct.Biol., 10, 104-108.
doi: 10.1038/nsb886.
- Abstract
- The L1 protuberance of the 50S ribosomal subunit is
implicated in the release/disposal of deacylated tRNA from
the E site. The apparent mobility of this ribosomal region
has thus far prevented an accurate determination of its
three-dimensional structure within either the 50S subunit
or the 70S ribosome. Here we report the crystal structure
at 2.65 A resolution of ribosomal protein L1 from
Sulfolobus acidocaldarius in complex with a specific
55-nucleotide fragment of 23S rRNA from Thermus
thermophilus. This structure fills a major gap in current
models of the 50S ribosomal subunit. The conformations of
L1 and of the rRNA fragment differ dramatically from those
within the crystallographic model of the T. thermophilus
70S ribosome. Incorporation of the L1-rRNA complex into the
structural models of the T. thermophilus 70S ribosome and
the Deinococcus radiodurans 50S subunit gives a reliable
representation of most of the L1 protuberance within the
ribosome.