Structure and ligand binding of the glutamine-II riboswitch
By Lin Huang, Jia Wang, Andrew M. Watkins, Rhiju Das, D. Lilley. 2019
21 citations recorded by the source corpus.
Abstract We have determined the structure of the glutamine-II riboswitch ligand binding domain using X-ray crystallography. The structure was solved using a novel combination of homology modeling and molecular replacement. The structure comprises three coaxial helical domains, the central one of which is a pseudoknot with partial triplex character. The major groove of this helix provides the binding site for L-glutamine, which is extensively hydrogen bonded to the RNA. Atomic mutation of the RNA at the ligand binding site leads to loss of binding shown by isothermal titration calorimetry, explaining the specificity of the riboswitch. A metal ion also plays an important role in ligand binding. This is directly bonded to a glutamine carboxylate oxygen atom, and its remaining inner-sphere water molecules make hydrogen bonding interactions with the RNA.
Subfields: Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
- Jack Hanson
- Kuldip K. Paliwal
- Yaoqi Zhou
- Jaswinder Singh
- Yuedong Yang
- Jinbo Xu
- Sheng Wang
- Thomas Litfin
Citations in the corpus
- Assessment of three-dimensional RNA structure prediction in CASP15 (2023, neutral): “76 While we began these explorations in studies described above to rank models based on agreement with x-ray data (Section 3.6), such scores based on optimal placements do not necessarily reflect models' value as search models for real-world Molecular Replacement (MR).”
- RNA secondary structure prediction using an ensemble of two-dimensional deep neural networks and transfer learning (2019, background): “For these two RNAs, experimental evidence suggests strand swapping in dimerization 44,45 .”