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2N0J

Solution NMR Structure of the 27 nucleotide engineered neomycin sensing riboswitch RNA-ribostamycin complex

Summary for 2N0J
Entry DOI10.2210/pdb2n0j/pdb
NMR InformationBMRB: 25526
DescriptorRNA_(27-MER), RIBOSTAMYCIN (2 entities in total)
Functional Keywordsriboswitches, rna-ligand interaction, aminoglycosides, rna recognition, rna structure, rna
Biological sourcesynthetic construct
Total number of polymer chains1
Total formula weight9011.50
Authors
Duchardt-Ferner, E.,Gottstein-Schmidtke, S.R.,Weigand, J.E.,Ohlenschlaeger, O.E.,Wurm, J.,Hammann, C.,Suess, B.,Woehnert, J. (deposition date: 2015-03-09, release date: 2016-02-03, Last modification date: 2024-05-01)
Primary citationDuchardt-Ferner, E.,Gottstein-Schmidtke, S.R.,Weigand, J.E.,Ohlenschlager, O.,Wurm, J.P.,Hammann, C.,Suess, B.,Wohnert, J.
What a Difference an OH Makes: Conformational Dynamics as the Basis for the Ligand Specificity of the Neomycin-Sensing Riboswitch.
Angew.Chem.Int.Ed.Engl., 55:1527-1530, 2016
Cited by
PubMed Abstract: To ensure appropriate metabolic regulation, riboswitches must discriminate efficiently between their target ligands and chemically similar molecules that are also present in the cell. A remarkable example of efficient ligand discrimination is a synthetic neomycin-sensing riboswitch. Paromomycin, which differs from neomycin only by the substitution of a single amino group with a hydroxy group, also binds but does not flip the riboswitch. Interestingly, the solution structures of the two riboswitch-ligand complexes are virtually identical. In this work, we demonstrate that the local loss of key intermolecular interactions at the substitution site is translated through a defined network of intramolecular interactions into global changes in RNA conformational dynamics. The remarkable specificity of this riboswitch is thus based on structural dynamics rather than static structural differences. In this respect, the neomycin riboswitch is a model for many of its natural counterparts.
PubMed: 26661511
DOI: 10.1002/anie.201507365
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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