Summary information and primary citation
- PDB-id
-
1jj2;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- ribosome
- Method
- X-ray (2.4 Å)
- Summary
- Fully refined crystal structure of the haloarcula
marismortui large ribosomal subunit at 2.4 angstrom
resolution
- Reference
-
Klein DJ, Schmeing TM, Moore PB, Steitz TA (2001):
"The
kink-turn: a new RNA secondary structure motif."
EMBO J., 20, 4214-4221. doi:
10.1093/emboj/20.15.4214.
- Abstract
- Analysis of the Haloarcula marismortui large ribosomal
subunit has revealed a common RNA structure that we call
the kink-turn, or K-turn. The six K-turns in H.marismortui
23S rRNA superimpose with an r.m.s.d. of 1.7 A. There are
two K-turns in the structure of Thermus thermophilus 16S
rRNA, and the structures of U4 snRNA and L30e mRNA
fragments form K-turns. The structure has a kink in the
phosphodiester backbone that causes a sharp turn in the RNA
helix. Its asymmetric internal loop is flanked by C-G base
pairs on one side and sheared G-A base pairs on the other,
with an A-minor interaction between these two helical
stems. A derived consensus secondary structure for the
K-turn includes 10 consensus nucleotides out of 15, and
predicts its presence in the 5'-UTR of L10 mRNA, helix 78
in Escherichia coli 23S rRNA and human RNase MRP. Five
K-turns in 23S rRNA interact with nine proteins. While the
observed K-turns interact with proteins of unrelated
structures in different ways, they interact with L7Ae and
two homologous proteins in the same way.