Abstract
The archaeal protein L7Ae forms part of a protein complex in the ribosome that specifically recognizes and binds to kink-turn RNA. In this complex, L7Ae directly interacts with the oligonucleotide and creates a functional arrangement for site-specific 2′-O-methylation. We report the solution NMR backbone assignment of Methanocaldococcus jannaschii L7Ae (117 residues, 12.7 kDa) in the ligand-free state and when bound to a 25 nucleotide C/D box kink-turn mimic RNA.
Highlights
The archaeal protein L7Ae forms part of a protein complex in the ribosome that recognizes and binds to kink-turn RNA
L7Ae directly interacts with the oligonucleotide and creates a functional arrangement for site-specific 20-O-methylation
We report the solution NMR backbone assignment of Methanocaldococcus jannaschii L7Ae (117 residues, 12.7 kDa) in the ligand-free state and when bound to a 25 nucleotide C/D box kink-turn mimic RNA
Summary
Abstract The archaeal protein L7Ae forms part of a protein complex in the ribosome that recognizes and binds to kink-turn RNA. We report the solution NMR backbone assignment of Methanocaldococcus jannaschii L7Ae (117 residues, 12.7 kDa) in the ligand-free state and when bound to a 25 nucleotide C/D box kink-turn mimic RNA. Keywords NMR Á Assignment Á L7Ae Á Kink-turn Á Ribosomal protein
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