NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA

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 bac...

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Autores principales: Moschen, Thomas, Wunderlich, Christoph, Kreutz, Christoph, Tollinger, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4351442/
https://www.ncbi.nlm.nih.gov/pubmed/25030110
http://dx.doi.org/10.1007/s12104-014-9569-8
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author Moschen, Thomas
Wunderlich, Christoph
Kreutz, Christoph
Tollinger, Martin
author_facet Moschen, Thomas
Wunderlich, Christoph
Kreutz, Christoph
Tollinger, Martin
author_sort Moschen, Thomas
collection PubMed
description 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.
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spelling pubmed-43514422015-03-11 NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA Moschen, Thomas Wunderlich, Christoph Kreutz, Christoph Tollinger, Martin Biomol NMR Assign Article 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. Springer Netherlands 2014-07-17 2015 /pmc/articles/PMC4351442/ /pubmed/25030110 http://dx.doi.org/10.1007/s12104-014-9569-8 Text en © The Author(s) 2014 https://creativecommons.org/licenses/by/4.0/ Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Article
Moschen, Thomas
Wunderlich, Christoph
Kreutz, Christoph
Tollinger, Martin
NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA
title NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA
title_full NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA
title_fullStr NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA
title_full_unstemmed NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA
title_short NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA
title_sort nmr resonance assignments of the archaeal ribosomal protein l7ae in the apo form and bound to a 25 nt rna
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4351442/
https://www.ncbi.nlm.nih.gov/pubmed/25030110
http://dx.doi.org/10.1007/s12104-014-9569-8
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