1JJ2

Fully Refined Crystal Structure of the Haloarcula marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution

Summary for 1JJ2

• Entry DOI: 10.2210/pdb1jj2/pdb
• Related: 1C04 1FFK
• Descriptor: 23S RRNA, RIBOSOMAL PROTEIN L10E, RIBOSOMAL PROTEIN L13, ... (36 entities in total)
• Functional Keywords: ribosome assembly, rna-rna, protein-rna, protein-protein, ribosome
• Biological source: Haloarcula marismortui; More
• Total number of polymer chains: 30
• Total formula weight: 1458155.19

Authors

Klein, D.J.,Schmeing, T.M.,Moore, P.B.,Steitz, T.A. (deposition date: 2001-07-03, release date: 2001-08-01, Last modification date: 2024-02-07)

Primary citation

Klein, D.J.,Schmeing, T.M.,Moore, P.B.,Steitz, T.A.
The kink-turn: a new RNA secondary structure motif.
EMBO J., 20:4214-4221, 2001

PubMed 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.

PubMed: 11483524
DOI: 10.1093/emboj/20.15.4214

Experimental method

X-RAY DIFFRACTION (2.4 Å)