4C4W

Structure of a rare, non-standard sequence k-turn bound by L7Ae protein

Summary for 4C4W

• Entry DOI: 10.2210/pdb4c4w/pdb
• Related: 4C40
• Descriptor: U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A, 50S RIBOSOMAL PROTEIN L7AE, TSKT-23, ... (4 entities in total)
• Functional Keywords: rna binding protein-rna complex, rna binding protein, kink turn, rna binding protein/rna
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus: P09012
• Total number of polymer chains: 8
• Total formula weight: 96595.42

Authors

Huang, L.,Lilley, D.M.J. (deposition date: 2013-09-09, release date: 2014-02-12, Last modification date: 2023-12-20)

Primary citation

Huang, L.,Lilley, D.M.J.
Structure of a Rare, Non-Standard Sequence K-Turn Bound by L7Ae Protein
Nucleic Acids Res., 42:4734-, 2014

PubMed Abstract: Kt-23 from Thelohania solenopsae is a rare RNA kink turn (k-turn) where an adenine replaces the normal guanine at the 2n position. L7Ae is a member of a strongly conserved family of proteins that bind a range of k-turn structures in the ribosome, box C/D and H/ACA small nucleolar RNAs and U4 small nuclear RNA. We have solved the crystal structure of T. solenopsae Kt-23 RNA bound to Archeoglobus fulgidus L7Ae protein at a resolution of 2.95 Å. The protein binds in the major groove displayed on the outer face of the k-turn, in a manner similar to complexes with standard k-turn structures. The k-turn adopts a standard N3 class conformation, with a single hydrogen bond from A2b N6 to A2n N3. This contrasts with the structure of the same sequence located in the SAM-I riboswitch, where it adopts an N1 structure, showing the inherent plasticity of k-turn structure. This potentially can affect any tertiary interactions in which the RNA participates.

PubMed: 24482444
DOI: 10.1093/NAR/GKU087

Experimental method

X-RAY DIFFRACTION (2.95 Å)