Summary information and primary citation
- PDB-id
-
1dk1;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- ribosome
- Method
- X-ray (2.8 Å)
- Summary
- Detailed view of a key element of the ribosome
assembly: crystal structure of the s15-rrna complex
- Reference
-
Nikulin A, Serganov A, Ennifar E, Tishchenko S, Nevskaya
N, Shepard W, Portier C, Garber M, Ehresmann B, Ehresmann
C, Nikonov S, Dumas P (2000): "Crystal
structure of the S15-rRNA complex."
Nat.Struct.Biol., 7, 273-277.
doi: 10.1038/74028.
- Abstract
- In bacterial ribosomes, the small (30S) ribosomal
subunit is composed of 16S rRNA and 21 distinct proteins.
Ribosomal protein S15 is of particular interest because it
binds primarily to 16S rRNA and is required for assembly of
the small subunit and for intersubunit association, thus
representing a key element in the assembly of a whole
ribosome. Here we report the 2.8 ¿ resolution crystal
structure of the highly conserved S15-rRNA complex. Protein
S15 interacts in the minor groove with a G-U/G-C motif and
a three-way junction. The latter is constrained by a
conserved base triple and stacking interactions, and locked
into place by magnesium ions and protein side chains,
mainly through interactions with the unique
three-dimensional geometry of the backbone. The present
structure gives insights into the dual role of S15 in
ribosome assembly and translational regulation.