Summary information and primary citation
- PDB-id
-
2yie;
SNAP-derived features in text and
JSON formats
- Class
- RNA
- Method
- X-ray (2.941 Å)
- Summary
- Crystal structure of a f. nucleatum fmn riboswitch
bound to fmn
- Reference
-
Vicens Q, Mondragon E, Batey RT (2011): "Molecular
Sensing by the Aptamer Domain of the Fmn Riboswitch: A
General Model for Ligand Binding by Conformational
Selection." Nucleic Acids Res.,
39, 8586. doi: 10.1093/NAR/GKR565.
- Abstract
- Understanding the nature of the free state of
riboswitch aptamers is important for illuminating common
themes in gene regulation by riboswitches. Prior evidence
indicated the flavin mononucleotide (FMN)-binding
riboswitch aptamer adopted a 'bound-like' structure in
absence of FMN, suggesting only local conformational
changes upon ligand binding. In the scope of pinpointing
the general nature of such changes at the nucleotide level,
we performed SHAPE mapping experiments using the aptamer
domain of two phylogenetic variants, both in absence and in
presence of FMN. We also solved the crystal structures of
one of these domains both free (3.3 Å resolution) and bound
to FMN (2.95 Å resolution). Our comparative study reveals
that structural rearrangements occurring upon binding are
restricted to a few of the joining regions that form the
binding pocket in both RNAs. This type of binding event
with minimal structural perturbations is reminiscent of
binding events by conformational selection encountered in
other riboswitches and various RNAs.
