ArticleNucleic acids research2014
Structure of a rare non-standard sequence k-turn bound by L7Ae protein.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
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- A general strategy for engineering GU base pairs to facilitate RNA crystallization.Nucleic acids research · 2025Article
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- Bacterial extracellular vesicles-based therapeutic strategies for bone and soft tissue tumors therapy.Theranostics · 2022Review
- Eukaryotic Box C/D methylation machinery has two non-symmetric protein assembly sites.Scientific reports · 2021Article
- Affinity and Structural Analysis of the U1A RNA Recognition Motif with Engineered Methionines to Improve Experimental Phasing.Crystals · 2021Article
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- Using sequence signatures and kink-turn motifs in knowledge-based statistical potentials for RNA structure prediction.Nucleic acids research · 2017Article
- The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.Biomolecules · 2016Review
- The solution structural ensembles of RNA kink-turn motifs and their protein complexes.Nature chemical biology · 2016Article
- The Kink Turn, a Key Architectural Element in RNA Structure.Journal of molecular biology · 2016Review
- The K-turn motif in riboswitches and other RNA species.Biochimica et biophysica acta · 2014Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
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.
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