title: NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA.
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.
authors.affiliation: Center for Molecular Biosciences Innsbruck (CMBI), Institute of Organic Chemistry, University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria.
authors.forename: Thomas
authors.initials: T
authors.lastname: Moschen
authors.forename: Christoph
authors.initials: C
authors.lastname: Wunderlich
authors.forename: Christoph
authors.initials: C
authors.lastname: Kreutz
authors.forename: Martin
authors.initials: M
authors.lastname: Tollinger
mesh_terms: D001059:Apoproteins / Q000737:chemistry* / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D063747:Methanocaldococcus; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D012313:RNA / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001059:Apoproteins; D019843:Archaeal Proteins; D012269:Ribosomal Proteins; D012313:RNA