1DK1

DETAILED VIEW OF A KEY ELEMENT OF THE RIBOSOME ASSEMBLY: CRYSTAL STRUCTURE OF THE S15-RRNA COMPLEX

Summary for 1DK1

• Entry DOI: 10.2210/pdb1dk1/pdb
• Descriptor: RRNA FRAGMENT, 30S RIBOSOMAL PROTEIN S15, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: ribosome, s15, protein, rna
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 2
• Total formula weight: 29267.49

Authors

Nikulin, A.,Serganov, A.,Ennifar, E.,Tischenko, S.,Nevskaya, N. (deposition date: 1999-12-06, release date: 2000-04-02, Last modification date: 2024-10-30)

Primary citation

Nikulin, A.,Serganov, A.,Ennifar, E.,Tishchenko, S.,Nevskaya, N.,Shepard, W.,Portier, C.,Garber, M.,Ehresmann, B.,Ehresmann, C.,Nikonov, S.,Dumas, P.
Crystal structure of the S15-rRNA complex.
Nat.Struct.Biol., 7:273-277, 2000

PubMed 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.

PubMed: 10742169
DOI: 10.1038/74028

Experimental method

X-RAY DIFFRACTION (2.8 Å)